ГИАЛУРОНИДАЗА И СПОСОБ ЕЕ ПРИМЕНЕНИЯ

Изобретение относится к области биохимии. Представлены выделенный белок гиалуронидазы, который имеет молекулярный вес приблизительно 44±1 кДа, содержащий аминокислотную последовательность, по меньшей мере, на 90% идентичную последовательности, которая содержит SEQ ID NO: I, SEQ ID NO: 2 и SEQ ID NO: 4, приведенные в описании, а также кодирующая его ДНК. Описан фармацевтический лекарственный состав для повышения проницаемости ткани или уменьшения вязкости соединительной ткани, содержащий эффективное количество выделенной указанной гиалуронидазы и фармацевтически приемлемый эксципиент, носитель, разбавитель или вспомогательный агент. Предложены способы: 1) предотвращения или минимизации образования рубца, включающий местное введение указанного фармацевтического состава; 2) сокращения проявления морщин посредством уменьшения вязкости соединительной ткани, включающие местное введение указанного фармацевтического состава; 3) облегчения дискомфорта или боли, вызванной ревматическим артритом, ...

ФАРМАЦЕВТИЧЕСКАЯ КОМПОЗИЦИЯ, ВКЛЮЧАЮЩАЯ ФЕРМЕНТ, РАЗРУШАЮЩИЙ ГЛИКОЗАМИНОГЛИКАНЫ, И ПРИМЕНЕНИЕ УКАЗАННОГО ФЕРМЕНТА ДЛЯ ПОЛУЧЕНИЯ ЛЕКАРСТВЕННОГО ПРЕПАРАТА ДЛЯ ТЕРАПИИ ГРЫЖИ МЕЖПОЗВОНОЧНОГО ДИСКА

Изобретение может быть использовано в медицине, а именно для терапии грыжи межпозвоночного диска. Фармацевтическая композиция для введения в вертебральное эпидуральное пространство включает фермент, разрушающий гликозаминогликаны, и фармацевтический носитель. Также изобретение относится к применению фермента, разрушающего гликозаминогликаны, в качестве лекарственного препарата для терапии грыжи межпозвоночного диска, который характеризуется наличием в эпидуральном пространстве студенистого ядра, где указанный препарат вводится в вертебральное эпидуральное пространство. Изобретение повышает эффективность терапии грыжи межпозвоночного диска. 2 с. и 11 з.п.ф-лы, 1 табл., 1 ил.

Способ лечения гиперкоррекции, возникающей при проведении контурной пластики гелями на основе гиалуроновой кислоты

Изобретение относится к медицине, а именно к косметологии. Выполняют локализацию дефекта с помощью ультразвукового исследования. Осуществляют коррекцию в 2 этапа, сначала воздействуют фонофорезом с 1% гидрокортизоновой мазью на соответствующую корригируемую зону, ежедневно по 4 минуты, курсом 6-10 сеансов. Затем через 3 недели проводят ультразвуковой (УЗ) контроль, после чего также под УЗ-контролем в участки нерастворившегося геля размером более 3 мм, обходя прилежащие сосуды и нервы, инъецируют «Лонгидазу» в дозе 75-150 ME. Через 2 недели выполняют повторное контрольное УЗ-исследование для подтверждения отсутствия участков нерастворившегося геля. Способ позволяет получить желаемый пациентом эстетический результат, сократить сроки медико-социальной реабилитации. 2 пр.

СПОСОБ ЛЕЧЕНИЯ ХРОНИЧЕСКОГО ПРОСТАТИТА

Способ лечения хронического простатита. Изобретение относится к медицине, а именно к урологии и может быть использовано при лечении хронического простатита. Цель изобретения - повышение терапевтической эффективности, за счет избирательного накопления препарата в области предстательной железы и профилактика осложнений за счет уменьшения его дозы. Сущность изобретения - вводят подкожно антибиотик в область проекции наружного отверстия пахового канала после предварительного введения лидазы.

СПОСОБ ЛЕЧЕНИЯ ХРОНИЧЕСКОГО КАЛЬКУЛЕЗНОГО ПРОСТАТИТА

Изобретение относится к медицине, а именно к урологии, и может быть использовано для лечения хронического калькулёзного простатита. Для этого осуществляют курс из 5-7 процедур трансректального ультразвукового воздействия в импульсном режиме, интенсивностью 0,2-0,4 Вт/смпо 5-7 минут ежедневно. Также проводят ферментотерапию препаратом Лонгидаза в дозе 3000 Ед 2 раза в неделю в течение 1 месяца. Кроме того, пациенту вводят ректальные суппозитории, содержащие 1000 мг Трилона Б и 200 мг димексида ежедневно на ночь в течение 3-х месяцев. При этом после выявления бактерий путём микроскопического и микробиологического исследования эякулята проводят антибактериальную терапию в течение 4-6 недель, вводя антибактериальный препарат согласно чувствительности к нему микрофлоры. Такое выполнение способа обеспечивает исчезновение камней в предстательной железе или уменьшение их количества, сокращение вероятности рецидивирования воспалительного процесса в предстательной железе, дифференцированный подход ...

Способ устранения рубцовых изменений кожи

Изобретение относится к медицине, а именно к дерматологии и дерматокосметологии, и может быть использовано для устранения рубцовых изменений кожи лба и щек. В качестве лекарственного препарата используют гиалуроновую кислоту путем ее инъекции до полного наполнения внутрирубцового объема с последующим повреждением микроиглами на глубину 1-2 мм рубцовой ткани с захватом здоровой ткани, до выхода крови в сформированные внутрирубцовые лакуны. Затем наносят на внешнюю поверхность рубца антисептик для образования корочки с последующим ее самоудалением. Проводят курс 8-10 процедур. Способ обеспечивает сокращение времени, необходимого для удаления рубцовой ткани, снижение травматизации кожи, уменьшение болевых ощущений и повышение скорости заживления обработанного участка за счет одновременного использования лекарственного препарата в сочетании с физическим фактором. 3 пр.

КРИСТАЛЛИЗОВАННАЯ ОКСАЛАТДЕКАРБОКСИЛАЗА И СПОСОБЫ ПРИМЕНЕНИЯ

... 1. Фармацевтическая композиция, содержащая кристалл оксалатдекарбоксилазы. ! 2. Композиция по п.1, в которой указанный кристалл более активен, чем растворимая форма оксалатдекарбоксилазы. ! 3. Композиция по п.2, в которой активность указанного кристалла является по меньшей мере приблизительно на 100% более высокой, чем активность растворимой формы при рН 4. ! 4. Композиция по п.1, в которой кристалл оксалатдекарбоксилазы поперечно-сшит сшивающим агентом и имеет по меньшей мере приблизительно 100% активности растворимой формы оксалатдекарбоксилазы. ! 5. Композиция по п.4, в которой кристалл оксалатдекарбоксилазы поперечно-сшит сшивающим агентом и имеет по меньшей мере приблизительно 150% активности растворимой формы оксалатдекарбоксилазы. ! 6. Композиция по п.4, в которой указанным сшивающим агентом является глутаральдегид. ! 7. Композиция по п.6, в которой кристалл оксалатдекарбоксилазы поперечно-сшит от приблизительно 0,02 % до приблизительно 1,5 % (вес./об.) глутаральдегида. ! 8. Композиция ...

CПOCOБ ЛEЧEHИЯ KOHИOTУБEPKУЛEЗA

Способ реабилитации организма человека после длительной обездвиженности

ISOLIERTE UND GEREINIGTE HUMANE LÖSLICHE GUANYLYLCYCLASE ALPHA1/BETA1 (hsGC ALPHA1/BETA1)

Materials and methods for the treatment of cns damage

CELLULOSE TRIACETATE ENZYME COMPLEX

Oligomeric peptides and their use for the treatment of hiv infections

Oligomeric peptides and their use for the treatment of hiv infections

Oligomeric peptides and their use for the treatment of hiv infections

PROCEDURE FOR THE PRODUCTION OF AN AQUEOUS DISPERSION OR LOESUNG OF AT A URETHANE POLYMERE BOUND PROTEIN

AUTOCIMMUNE REACTION CAUSING GAD65 OF PEPTIDE

STABLE NOT AQUEOUS ONES SINGLE-PHASE ONE VISCOUS ONES VEHICLES AND FORMULATIONS THIS VEHICLES USING

SPHINGOSIN-1-PHOSPHAT-LYASE OF POLYPEPTIDE, POLYNUKLEOTIDE AND MODULATING MEANS, AND PROCEDURES FOR THEIR USE

RATIONALLY DESIGNED ONE, LYASEN DERIVED FROM CHONDROITINASE B

BAKTERIOPHAGE FOR THE TREATMENT OF BACTERIAL BIO FILMS

USE OF HCG FRAGMENTS CONTAINED COMPOSITIONS TO MUKOSALEN AND ORAL APPLICATION

USE OF ADENYLZYCLASE AS VAKZIN APPROXIMATELY BORDETELLA.

KLONIERTE GLUTAMINSÄUREDEKARBOXYLASE

HEPARANASE SPECIFIC MOLECULAR PROBES AS WELL AS THEIR USE IN RESEARCH AND MEDICAL APPLICATIONS

POTASSIUM CHANNEL PROTEINS FOR USE IN GENE THERAPY FOR THE REDUCTION OF MORE EREKTILER DYSFUNKTION

PROCEDURE FOR THE SELECTIVE ONE METHIONINENTZUG FOR MALIGNANT MAMMALIAN CELLS

PHARMACEUTICAL DICLOFENAC CONNECTION BASED ON VITAMIN E, PAPAIN AND HYALURONIDASE

Regulation of human ornithine decarboxylase

Treatment of autoimmune disease using tolerization in combination with methotrexate

Phenylalanine ammonia lyase polypeptide and polynucleotide sequences and methods of obtaining and using same

Treatment of central nervous system damage

The tuberculosis Rv2386c protein, compositions and uses thereof

Polypeptide mixes with antibacterial activity

The invention relates to the field of microbiology, specifically to a combination of a source of a first enzymatic active domain and a source of a second enzymatic active domain and to a composition comprising said combination. The invention further relates to a composition comprising said combination for use as a medicament, to the use of said composition as an antimicrobial agent and to a method for controlling microbial contamination in a food-or feed product, on and/or in food-or feed processing equipment, on and/or in food-or feed containers.

Compositions and methods for treatment of homocystinuria

Provided are compositions and methods for enzyme replacement therapy using modified human cystathionine beta synthase (CBS) in the treatment of homocystinuria and related diseases and disorders.

Cloned glutamic acid decarboxylase

Carbonyl stress-ameliorating agents

Attenuation of fibroblast proliferation

Attenuation of tumor growth, metastasis and angiogenesis

COMPOSITION FOR REDUCING THE PHENYLALANINE BLOOD-LEVEL

Biochemical methods that eliminate corneal scars, opacification and haze

METHOD AND COMPOSITION FOR PROTECTING NEURONAL TISSUE FROM DAMAGE INDUCED BY ELEVATED GLUTAMATE LEVELS

A method of reducing extracellular brain glutamate levels. The method comprises administering to a subject in need thereof a therapeutically effective amount of an agent capable of reducing blood glutamate levels thereby reducing extracellular brain glutamate levels.

COMPOSITIONS AND METHODS FOR TREATMENT OF NEOVASCULAR DISEASES

PECTATE LYASES, NUCLEIC ACIDS ENCODING THEM AND METHODS FOR MAKING AND USING THEM

... ²²²The invention is directed to polypeptides having pectate lyase (pectinase) ²activity, polynucleotides encoding the polypeptides, and methods for making ²and using these polynucleotides and polypeptides. The polypeptides of the ²invention can be used as pectate lyases to catalyze the beta-elimination or ²hydrolysis of pectin and/or polygalacturonic acid, such as 1,4-linked alpha-D-²galacturonic acid. The invention provides methods of treating fibers, fabrics ²or any pectate- or polygalacturonic acid-comprising material using one or more ²pectate lyases of the invention.² ...

VARIANTS AND CHEMICALLY-MODIFIED VARIANTS OF PHENYLALANINE AMMONIA-LYASE

IMMUNOREACTIVE AND IMMUNOTHERAPEUTIC MOLECULES WHICH INTERACT IN SUBJECTS WITH INSULIN-DEPENDENT DIABETES MELLITUS (IDDM)

COMPOSITIONS AND METHODS FOR THE TREATMENT OF PARKINSON'S DISEASE

The present disclosure relates to methods, formulations and devices for the delivery and therapeutic administration of polynucleotides encoding AADC. The present disclosure relates to methods, formulations and devices for the delivery and therapeutic administration of AAV vectors which include polynucleotides encoding AADC. The present disclosure relates to methods, formulations and devices for the delivery7 and therapeutic administration of polynucleotides encoding AADC in the treatment of neurological diseases, disorders and conditions, including Parkinson's Disease.

METHOD OF TREATING A MAMMAL, INCLUDING HUMAN, AGAINST CANCER USING METHIONINE AND ASPARAGINE DEPLETION

The invention is related to a new method for treating liquid and solid cancers, in a mammal, including human, wherein methioninase is administered before asparaginase. The invention also encompasses the use of a dietary methionine deprivation, possibly combined with methioninase administration, in advance of asparaginase treatment. Methioninase and asparaginase may be used in particular under free form, pegylated form or encapsulated into erythrocytes.

METHODS AND COMPOSITIONS FOR TREATING ERECTILE DYSFUNCTION

Methods are provided for increasing libido and/or treating erectile dysfunction in a man. The methods include the administration of a formulation testosterone alone, another fast-acting drug to treat erectile dysfunction or a combination of the testosterone and the other drug where at least one is delivered by aersolization. The formulation is preferably aerosolized and inhaled into a patient's lungs where particles of testosterone and/or the fast- acting erectile dysfunction drug deposits on lung tissue and then enter the patient's circulatory system.

MATERIALS AND METHODS FOR PREVENTION AND TREATMENT OF RNA VIRAL DISEASES

The subject invention concerns a method of inhibiting an RNA virus infection within a patient by increasing the amount of 2-5 oligoadenylate (2-5 AS) activity within the patient. Preferably, the preventive and therapeutic methods of the present invention involve administering a nucleotide encoding 2- 5 AS, or at least one catalytically active fragment thereof, such as the p40, p69, p100 subunits to a patient in need thereof. The present inventors have determined that overexpression of 2-5AS causes a reduction in epithelial cell damage, reduction in infiltration of mononuclear cells in the peribronchiolar and perivascular regions, and reduction in thickening of the septa in the lungs. Levels of chemokines, such as MIP1-.alpha., are also reduced upon overexpression of 2-5AS. The subject invention also pertains to pharmaceutical compositions containing a nucleotide sequence encoding 2-5AS and pharmaceutically acceptable carrier, as well as vectors for delivery of the 2- 5AS nucleotide sequence ...

PECTATE LYASES, NUCLEIC ACIDS ENCODING THEM AND METHODS FOR MAKING AND USING THEM

The invention is directed to polypeptides having pectate lyase (pectinase) activity, polynucleotides encoding the polypeptides, and methods for making and using these polynucleotides and polypeptides. The polypeptides of the invention can be used as pectate lyases to catalyze the beta-elimination or hydrolysis of pectin and/or polygalacturonic acid, such as 1,4-linked alpha-D- galacturonic acid. The invention provides methods of treating fibers, fabrics or any pectate- or polygalacturonic acid-comprising material using one or more pectate lyases of the invention.

DICLOFENAC PHARMACEUTICAL COMPOSITION BASED ON VITAMIN-E, PAPAIN AND HYALURONIDASE

The present application refers to a new pharmaceutical composition of diclofenac comprising the following formulation: PAPAIN ...0.1 to 15 %, HYALURONIDASE ...50 to 900 utr/mg, VITAMIN E ...10 to 2000 mg.

PRODUCTION OF RHPBGD AND NEW THERAPEUTIC METHODS FOR TREATING PATIENTS WITH ACUTE INTERMITTENT PORPHYRIA (AIP) AND OTHER PORPHYRIC DISEASES

A method for production of rhPBGD in high scale and use of rhPBGD in a method for treatment or prophylaxis of disease caused by deficiency, in a subject, of an enzyme belonging to the heme biosynthetic pathway. The method comprising administering, to the subject, an effective amount of one or more catalyst which is said enzyme or an enzymatically equivalent part or analogue thereof prefreable in combination with a gene therapy of a mutation related to the catalyst. The disease is selected from the group consisting of acute intermittent porphyria (AIP), ALA deficiency porphyria (ADP), Porphyria cutanea tarda (PCT), Hereditary coproporphyria (HCP), Harderoporphyria (HDP), Variegata porphyria (VP), Congenital erythropoietic porphyria (CEP), Erythropoietic protoporphyria (EPP), and Hepatoerythropoietic porphyria (HEP). The catalyst is one or more enzymes selected from the group consisting of delta-aminolevulininic acid synthetase, delta-aminovulinic acid dehydratase (ALAD), porphobilinogen ...

ENGINEERED PHENYLALANINE AMMONIA LYASE POLYPEPTIDES

The present invention provides engineered phenylalanine ammonia lyase (PAL) polypeptides and compositions thereof, as well as polynucleotides encoding the engineered phenylalanine ammonia lyase (PAL) polypeptides. In some embodiments, the engineered PAL polypeptides are optimized to provide enhanced catalytic activity, as well as reduced sensitivity to proteolysis and increased tolerance to storage at elevated temperatures. In some embodiments, the engineered PAL polypeptides contain fewer phenylalanine residues than wild-type PAL polypeptides. The present invention also provides methods for the use of the compositions comprising the engineered PAL polypeptides for therapeutic and industrial purposes.

COMPOSITION AND METHOD FOR PREVENTION AND TREATMENT OF TYPE I DIABETES

A composition for the prevention or treatment of type I diabetes in a sub ject, said composition comprising a fusion protein selected from the group c onsisting of GLP-1/IgG or variant or fragment thereof and an Ex4/IgG or vari ant or fragment thereof and an autoimmune suppressor for silencing an autoim mune response against islet beta cells.

FUSION PROTEINS FOR THE TREATMENT OF CNS

This disclosure relates to compositions capable of use in the treatment of spinal cord injuries and related disorders of the central nervous system (CNS), and in particular, compositions including proteoglycan degrading molecules and compositions capable of blocking and/or over coming the activity of neuronal growth inhibitory molecules, as well as fusion proteins which includes a proteoglycan degrading domain and a domain capable of blocking and or over coming the activity of neuronal growth inhibitory molecules.

ENGINEERED ENZYMES WITH METHIONINE-GAMMA-LYASE ENZYMES AND PHARMACOLOGICAL PREPARATIONS THEROF

Methods and composition related to the engineering of a novel protein with methionine-?-lyase enzyme activity are described. For example, in certain aspects there may be disclosed a modified cystathionine-?-lyase (CGL) comprising one or more amino acid substitutions and capable of degrading methionine. Furthermore, certain aspects of the invention provide compositions and methods for the treatment of cancer with methionine depletion using the disclosed proteins or nucleic acids.

ATTENUATION OF TUMOR GROWTH, METASTASIS AND ANGIOGENESIS BY USE OF CHONDROITIN SULFATE DEGRADING ENZYMES

A highly purified and specific glycosaminoglycan degrading enzyme, chondroitinase AC, and to a lesser extent, chondroitinase B, can be used in the treatment of metastatic cancers and in other disorders characterized by angiogenesis. The enzymatic removal of chondroitin sulfates A and C, and to a lesser extent, chondroitin sulfate B, from cell surfaces directly decreases the ability of tumor cells to invade blood vessels and thus prevents the formation of metastatic, or secondary tumors; inhibits tumor cell growth; and decreases angiogenesis by inhibiting both endothelial cell proliferation and capillary formation. Decreasing the formation of new blood vessels into the tumor in turn decreases the potential for tumor growth, and further decreases the ability of tumor cells to invade the bloodstream. These effects are opposite to the pro-metastatic effects of tumor-secreted heparanase.

POLYNUCLEOTIDE ENCODING A POLYPEPTIDE HAVING HEPARANASE ACTIVITY AND EXPRESSION OF SAME IN TRANSDUCED CELLS

A polynucleotide (hpa) encoding a polypeptide having heparanase activity, vectors including same, transduced cells expressing heparanase and a recombinant protein having heparanase activity.

Therapeutic compositions for treating deposits of excess fat and infiltrates causing cellulite

Process for the preparation of an aqueous dispersion or solution of a protein bonded to a urethane polymer

NOVEL COMPOSITION, IN PARTICULAR FOR THE TREATMENT OF CELLULITE.

Method for suppressing the immunogenic action of a biocatalyst.

Method for selective methionine starvation of malignant cells in mammals

CONSTRUCTED POLYPEPTIDES-PHENYLALANINE - AMMIAKLIAZY

КОМПОЗИЦИЯ ДЛЯ СТАБИЛИЗАЦИИ ГИАЛУРОНИДАЗЫ И ЕЕ ПРИМЕНЕНИЕ

Предусмотрены композиции, содержащие растворимую гиалуронидазу и Lys-Lys в количестве, обеспечивающем стабильность гиалуронидазы и содержащих ее композиций.

TUBERCULOSIS PROTEIN RV2386C, COMPOSITIONS AND THEIR APPLICATIONS

IN VIVO OF FIELD KhONDROITINAZY AND/OR HYALURONIDASE FOR IMPROVEMENT OF DELIVERY AGENT

Antitumor and anticholesterol preparations containing a lipoteichoic acid from steptococcus

Purification and isolation of recombinant oxalate degrading enzymes and spray-dried particles containing oxalate degrading enzymes

THE USE OF PREPARATIONS BASED ON VACCINATING OF ADENYL CYCLASE OR BACTERIA THAT PRODUCE THEM AS PROTECTIVE ANTIGENS AGAINST THE EFFECTS OF BORDETELLA

Cosmetic/pharmaceutical composition, useful e.g. to protect skin and integument against all types of external aggressions and to prevent\treat signs of skin aging and/or photo-aging, comprises polypeptide derived from aconitase enzyme

La présente invention concerne une composition cosmétique ou pharmaceutique, et notamment dermatologique, comprenant dans un milieu physiologiquement adapté, des peptides dérivés de l'enzyme aconitase, en tant qu'agents actifs, seuls ou en association avec au moins un autre agent actif. L'invention est également relative à l'utilisation cosmétique d'une composition protectrice des mitochondries. L'invention porte encore sur un procédé de traitement cosmétique destiné à protéger la peau et les phanères des agressions extérieures et à lutter contre le vieillissement cutané.

SUPER FAST-ACTING INSULIN COMPOSITIONS

Homo compositions and method for the treatment

... 호모시스틴뇨증 및 관련 질환 및 장애의 치료에서 변형된 인간 시스타티오닌 베타 신타제(CBS)를 이용한 효소 대체 요법을 위한 조성물 및 방법이 제공된다.

Pharmaceutical composition for reducing oxalate levels in a patient

A method for reducing oxalate levels in a patient that includes administering to the patient a therapeutically effective amount of non-absorbable amine polymers such as a polymer characterized by a repeat unit having the formula, and salts and copolymers thereof, where n is a positive integer and x is zero or an integer between 1 and about 4.

SPHINGOSINE-1-PHOSPHATE LYASE POLYPEPTIDES, POLYNUCLEOTIDES AND MODULATING AGENTS AND METHODS OF USE THEREFOR

Compositions, methods and kits for diagnosing and treating cancer are provided. Therapeutic compositions may comprise agents that modulate the expression or activity of a sphingosine-1-phosphate lyase (SPL). Such compositions may be administered to a mammal afflicted with cancer. Diagnostic methods and kits may employ an agent suitable for detecting alterations in endogenous SPL. Such methods and kits may be used to detect the presence of a cancer or to evaluate the prognosis of a known disease. SPL polypeptides, polynucleotides and antibodies are also provided.

SITE-SPECIFIC IN SITU GENERATION OF ALLICIN USING A TARGETED ALLIINASE DELIVERY SYSTEM FOR THE TREATMENT OF CANCERS, TUMORS, INFECTIOUS DISEASES AND OTHER ALLICIN-SENSITIVE DISEASES

Conjugates of the enzyme alliinase with a protein carrier that targets the alliinase to specific cells are used in combination with alliin to produce allicin at a desired target site. The enzyme converts alliin to allicin at the target site to kill cancer cells or pathogens.

DSP-18 DUAL-SPECIFICITY PHOSPHATASE

Compositions and methods are provided for the treatment of conditions associated with cell proliferation, cell differentiation and/or cell survival. In particular, the dual-specificity phosphatase DSP-18 isoforms DSP-18a-f, and polypeptide variants thereof that stimulate dephosphorylation of DSP-18 substrates, are provided. The polypeptides may be used, for example, to identify antibodies and other agents that inhibit DSP-18 activity. The polypeptides and agents may be used to modulate cell proliferation, cell differentiation and cell survival.

HEPARINASE III AND USES THEREOF

The invention relates to heparinase III and mutants thereof. Modified forms of heparinase III having reduced enzymatic activity which are useful for a variety of purposes, including sequencing of heparin-like glycosaminoglycans (HLGAGs), removing active heparan sulfate from a solution, inhibition of angiogenesis, etc. have been discovered according to the invention. The invention in other aspects relates to methods of treating cancer and inhibiting tumor cell growth and/or metastasis using heparinase III, or products produced by enzymatic cleavage by heparinase III of HLGAGs.

THERAPEUTIC AGENT FOR DISC HERNIATION

The present invention provides a therapeutic agent for disc herniation, which has extremely few adverse side effects, can achieve a prolonged pain-ameliorating effect when administered in only a single dose, and can exhibit a high therapeutic effect and high safety in clinical applications. The present invention relates to a therapeutic agent for disc herniation, which is characterized by containing chondroitinase ABC as an active ingredient and being administered in such a manner that the ingredient can be administered into a human disk in an amount of 1-8 units per disk.

Compositions for the Restoration of a Fecal Microbiota and Methods for Making and Using Them

In alternative embodiments, the invention provides compositions and methods for treating various disorders and conditions in mammals, including chronic disorders in which there is a presence of an abnormal microbiota or an abnormal distribution of microflora in the gastrointestinal tract. In alternative embodiments, the invention provides liquid preparations or formulations derived from a human fecal material (e.g., a stool) processed, e.g., filtered and/or centrifuged, such that all bacteria, fungal spores and viruses are removed, but retaining the native biologically active molecules from the fecal material and bacteriophages. In alternative embodiments, the invention provides a “rough-”, “incomplete-” or medium-filtered microbiota which still comprises native physiological components or nutritive agents for the bacteria, e.g., retains native biologically and nutritionally active components. In alternative embodiments, the invention provides a highly filtered or substantially purified ...

Biological control of crown gall disease on grapevines

Derivatives of Agrobacterium vitis strain F2/5 are disclosed. These derivatives were generated following homologous recombination with an internal fragment of targeted genes resulting in gene disruption by insertion of a copy of suicide vector pVIK165. The genes disrupted were F-avi5813 encoding a phosphopantetheinyltransferase, F-avi4329 encoding an aminotransferase and F-avi0838 (rirA) encoding an iron responsive transcriptional regulator. Such derivatives control crown gall on grapevines. In addition, these derivatives did not induce roots necrosis but enhanced root development and callus formation. On young stem explants, it was shown as well that the F2/5 derivatives are necrosis-negative.

METHOD OF TREATING A MAMMAL, INCLUDING HUMAN, AGAINST CANCER USING METHIONINE AND ASPARAGINE DEPLETION

The invention is related to a new method for treating liquid and solid cancers, in a mammal, including human, wherein methioninase is administered before asparaginase. The invention also encompasses the use of a dietary methionine deprivation, possibly combined with methioninase administration, in advance of asparaginase treatment. Methioninase and asparaginase may be used in particular under free form, pegylated form or encapsulated into erythrocytes.

Phenylalanine ammonia lyase occluded fibers for reducing phenylalanine blood-level

Phenylalanine level in blood or another medium is considerably reduced and can even be annulled by causing blood or the other medium to flow through a mass of porous fibers in which the enzyme phenylalanine ammonia lyase has been occluded: the fibers have been previously made biocompatible, if necessary.

CYCLE ADENOSINE MONOPHOSPHATE-INCOMPETENT ADENYLYL CYCLASE AND COMPOSITIONS AND METHODS FOR TREATING HEART FAILURE AND INCREASING CARDIAC FUNCTION

The invention provides methods for treating, ameliorating or protecting (preventing) an individual or a patient having or at risk of having heart disease or heart failure, or decreased cardiac function, comprising: providing a cyclic adenosine monophosphate-incompetent (cAMP-incompetent) adenylyl cyclase type 6 (AC6) protein or polypeptide (also called “an AC6mut”), or an AC6mut-encoding nucleic acid or a gene operatively linked to a transcriptional regulatory sequence.

Compositions of prokaryotic phenylalanine ammonia-lyase and methods of using compositions thereof

The present invention is directed to phenylalanine ammonia-lyase (PAL) produced by prokaryotes, wherein such prokaryotic PAL wherein the PAL variant has a greater phenylalanine-converting activity and/or a reduced immunogenicity as compared to a wild-type PAL. The invention thus provides compositions of bacterial PAL and biologically active fragments, mutants, variants and analogs thereof, as well as methods for the production, purification, and use of such compositions for therapeutic and industrial purposes.

Chorismate synthase

The invention provides aroC polypeptides and polynucleotides encoding aroC polypeptides and methods for producing such polypeptides by recombinant techniques. Also provided are methods for utilizing aroC polypeptides to screen for antibacterial compounds.

Способ получения фермента метионин-гамма-лиазы, противоопухолевое лекарственное средство ГЛФ МГЛ на основе этого фермента и применение этого средства для торможения роста опухоли (варианты)

Изобретение относится к области биотехнологии. Разработан способ получения фермента метионин-гамма-лиазы (МГЛ) и противоопухолевое лекарственное средство ГЛФ МГЛ на основе этого фермента. Способ с использованием штамма Е.coli MDG1216 позволяет синтезировать до 45% МГЛ, в расчете на суммарный клеточный белок, с удельной активностью от 15 до 32 ед./мг с Kmпорядка 0,7±0,11 mM в реакциях γ-элиминирования для природного субстрата L-метионина. Заявляемое лекарственное средство ГЛФ МГЛ обладает противоопухолевым эффектом (более 50% ТРО), что продемонстрировано при применении его для торможения роста опухоли - меланома В 16 - путем комбинированной терапии в сочетании с пиридоксином, а также для торможения роста опухоли - немелкоклеточный рак легкого человека - путем комбинированной терапии в сочетании с дексорубицином. 2 н.п. ф-лы, 3 ил., 4 пр., 2 табл.

КОМПОЗИЦИЯ ДЛЯ ОБЛЕГЧЕНИЯ ИЛИ ЛЕЧЕНИЯ БОЛИ

Настоящее изобретение относится к области биотехнологии, конкретно к генам, операбельно связанным в векторе, и может быть использовано в медицине для облегчения или лечения боли. Предложена фармацевтическая композиция, содержащая эффективное количество двух или более генов, выбранных из группы, состоящей из гена, кодирующего глутаматдекарбоксилазу (GAD), гена, кодирующего интерлейкин-10 (IL-10), и гена, кодирующего глиальный нейротрофический фактор (GDNF). Гены в композиции находятся в операбельном виде в векторе. Изобретение обеспечивает высокий анальгетический эффект при введении сочетания генов в дозировке ниже, чем при введении генов по отдельности, и, таким образом, обычные побочные эффекты и токсичность могут быть снижены. 4 н. и 14 з.п. ф-лы, 7 табл., 7 пр., 15 ил.

Способ лимфатической терапии при панкреатитах у собак

Изобретение относится к области ветеринарии и представляет собой способ терапии собак с панкреатитами, характеризующийся назначением в сочетании с традиционной терапией комплекса лимфостимулирующих инъекций в толщу межостистой связки позвоночника на уровне L-III-L-IV свежеприготовленной лекарственной смеси, содержащей 2 мл 5%-го раствора Мексидол-Вет® 5%-го, 15 ЕД лидазы, 1 мл 2%-го раствора лидокаина, 1 мл 40%-го раствора глюкозы и 1 мл 0,9%-го раствора натрия хлорида в дозе 0,5 мл на 1 кг массы животного 5 раз с интервалом 24 часа. Изобретение обеспечивает возможность повышения эффективности терапии при панкреатитах у собак и кошек за счет усиления микроциркуляции, лимфодренажа и устранения отечности поджелудочной железы, скорейшего очищения патологического очага от вредных продуктов распада тканей, микробов и их токсинов, повышение устойчивости организма к воздействию свободных радикалов и повреждающих факторов, приводящих к кислородозависящим патологическим состояниям, а также ускорения ...

Способ профилактики рубцово-склеротических осложнений после оперативного лечения на верхних мочевых путях

Изобретение относится к медицине, а именно к урологии и физиотерапии, и может быть использовано для профилактики рубцово-склеротических осложнений после оперативного лечения на верхних мочевых путях. Для этого проводят дренирование верхних мочевых путей путём чрескожной пункционной нефростомии, антибиотикопрофилактику. Внутримышечно вводят Лонгидазу 3000 ME 1 раз в 3 дня курсом 10 инъекций. Начиная со следующих суток после установки нефростомического дренажа осуществляют наружную магнитно-лазерную терапию в количестве 10 процедур. На 7 сутки после установки нефростомического дренажа проводят курс многоканальной электростимуляции (МЭС) в областях трапециевидной и широчайших мышц спины, прямой и косых мышц живота биполярно-импульсными токами с трапециевидной огибающей частотой 1-150 Гц, посылкой и паузой по 2 с, временем воздействия 15-20 минут. МЭС сочетают с ультрафонофорезом Лонгидазы 3000 ME в проекции пораженного мочеточника с интенсивностью 0,2 Вт/смв непрерывном режиме лабильно. Курс ...

СПОСОБ ОСУЩЕСТВЛЕНИЯ СЕЛЕКТИВНОГО МЕТИОНИНОВОГО ГОЛОДАНИЯ КЛЕТОК В ОРГАНИЗМЕ МЛЕКОПИТАЮЩЕГО, ПОЛИНУКЛЕОТИД, КАТАЛИТИЧЕСКИ АКТИВНЫЙ ПОЛИПЕПТИД РЕКОМБИНАНТНОЙ МЕТАЗЫ

Изобретение относится к области медицины. В частности, описан усовершенствованный способ химиотерапии злокачественных клеток млекопитающих, которые имеют абсолютную потребность в метионине, но не содержат метилтиоаденозинфосфорилазу (МТАазу). Способ предусматривает детекцию МТАза-отрицательных клеток в организме млекопитающих, введение метионин-y-лиазы в достаточном количестве для снижения объема МТАаза-отрицательных клеток в организме млекопитающего и совместное введение метилтиоаденозина в количестве, достаточном для постоянной доступности метионина для незлокачественных клеток млекопитающего. Предложены также каталитически активный полипептид рекомбинантной МЕТазы и полинуклеотид, кодирующий этот полипептид. Технический результат изобретения - расширение арсенала средств для борьбы со злокачественными клетками. 3 с. и 17 з.п. ф-лы, 2 табл., 4 фиг.

Способ получения фермента метионин-гамма-лиазы, противоопухолевое лекарственное средство ГЛФ МГЛ на основе этого фермента и применение этого средства для торможения роста опухоли (варианты)

СПОСОБ ОБЕСПЕЧЕНИЯ ТРЕБУЕМЫХ УРОВНЕЙ ФАКТОРА 2 РОСТА ГЛИИ В ПЛАЗМЕ

СПОСОБ ЛЕЧЕНИЯ ОСТРОГО ПОСЛЕРОДОВОГО ЭНДОМЕТРИТА

Изобретение относится к медицине, а именно к акушерству и гинекологии, и может быть использовано для лечения острого послеродового эндометрита. Для этого в 2 этапа проводят регионарную антибактериальную терапию. На 1-м этапе в область паховых регионарных лимфатических узлов подкожно вводят комбинации лекарственных препаратов: лидазы 16 ЕД+1 мл 2% р-ра лидокаина гидрохлорида. После этого, не вынимая иглы, в эту же область вводят 0,5 г цефтриаксона в 1 мл 2% р-ра лидокаина гидрохлорида. На 2-м этапе регионарную лимфотропную терапию осуществляют путём проведения низкочастотного ультразвука. Для этого на кожу в области проекции поверхностного кольца паховых каналов помещают марлевые тампоны размером 10×10 см, смоченные лекарственной смесью, включающей раствор лидазы 16 ЕД+1 мл 2% р-ра лидокаина гидрохлорида и 0,5 г цефтриаксона. При этом ультрафонофорез этой зоны осуществляют в течение 25 секунд с частотой 0,88 МГц. Курс лечения составляет 5 ежедневных процедур. Способ обеспечивает предупреждение ...

Способ лечения острой ишемии миокарда

СПОСОБ ЛЕЧЕНИЯ ОСТРОЙ ИШЕМИИ МИОКАРДА путем внутрикоронарного или внутривенного введения стрептокиназы, отличающийся тем, что, с целью предупреждения необратимых микрососудистых изменений в зоне ишемии, пред варительно, не позднее 24 ч от начала острого ангинозного приступа, больным вводят ингибитор протеаз контрикал в сочетании с гепарином в соотношении не менее 3:1, а стрептокиназу вводят через 1 -1,5 ч после окончания инфузии указанной смеси.

Способ лечения кониотуберкулеза

Изобретение относится к медицине, в частности к пульмонологии. Цель - сокращение сроков лечения обострения процесса и предупреждение рецидива заболевания у больных с лимфобронхиальными свищами. Для этого эндобронхиальным путем вводят рифампицин с гидрокортизоном в течение 2-х дней, тубазид, токоферол и лидазу на 3-й день и повторяют чередование препаратов в течение 1 мес.

ENZYMATIC NEUTRALIZATION OF HEPARIN

Homolactic Fermentation from Pentose

Provided is a lactic acid bacterium capable of homolactic fermentation using a pentose as a substrate, the lactic acid bacterium utilizing a pentose, and in which a phosphoketolase pathway is blocked and a pentose phosphate pathway is activated. Also provided is a method for producing lactic acid from a pentose using the lactic acid bacterium and a method for preparing the lactic acid bacterium.

Novel Sesquiterpene Synthase Gene and Protein

The invention relates to sesquiterpene synthases and methods for their production and use. Particularly, the invention provides nucleic acids comprising the nucleotide sequence of citrus valencene synthase (CVS) which codes for at least one CVS. The invention further provides nucleic acids comprising the nucleotide sequence coding for amino acid residues forming the tier 1 and tier 2 domains of CVS. The invention also provides for methods of making and using the nucleic acids and amino acids of the current invention.

Compositions and methods for promoting neuronal outgrowth

Neural outgrowth in the central nervous system is achieved by administering chondroitinase AC and/or chondroitinase B to degrade chondroitin sulfate proteoglycans that inhibit or contribute to the inhibition of nervous tissue regeneration.

Recombinant Halohydrin Dehalogenase Polypeptides

The present disclosure provides engineered halohydrin dehalogenase (HHDH) polypeptides having improved enzyme properties as compared to the wild-type HHDH enzyme HheC and other reference engineered HHDH polypeptides. Also provided are polynucleotides encoding the engineered HHDH enzymes, host cells capable of expressing the engineered HHDH enzymes, and methods of using the engineered HHDH enzymes to synthesize a variety of chiral compounds including chiral epoxides and chiral alcohols.

Isoprene synthase variants for improved production of isoprene

The present invention provides methods and compositions comprising at least one isoprene synthase enzyme with improved specific productivity. In particular, the present invention provides variant plant isoprene synthases for increased isoprene production in host cells.

Chimeric isoprenoid synthases and uses thereof

Provided is a chimeric isoprenoid synthase polypeptide including a first domain from a first isoprenoid synthase joined to a second domain from a second, heterologous, isoprenoid synthase, whereby the chimeric isoprenoid synthase is capable of catalyzing the production of isoprenoid reaction products that are not produced in the absence of the second domain of the second, heterologous, isoprenoid synthase. Also provided is a chimeric isoprenoid synthase polypeptide including an asymmetrically positioned heterologous domain, whereby the chimeric isoprenoid synthase is capable of catalyzing the production of isoprenoid reaction products that are not produced when the domain is positioned at its naturally-occurring site in the isoprenoid synthase polypeptide. 1. A method for producing a chimeric isoprenoid synthase polypeptide , comprising:(a) providing a cell comprising DNA encoding the chimeric isoprenoid synthase polypeptide, wherein the encoded synthase comprises a first sesquiterpene isoprenoid synthase polypeptide domain joined to a second, different, sesquiterpene isoprenoid synthase polypeptide domain such that the chimeric isoprenoid synthase polypeptide produces one or more isoprenoid products that are not produced in the absence of the second domain of the second synthase;(b) culturing said cell under conditions for expressing the DNA to produce the chimeric isoprenoid synthase; and(c) recovering the chimeric isoprenoid synthase.2. The method of claim 1 , wherein the encoded chimeric isoprenoid synthase comprises a first isoprenoid sesquiterpene synthase polypeptide domain joined to a second different isoprenoid sesquiterpene synthase polypeptide domain claim 1 , interrupted by or including a ratio determinant domain claim 1 , whereby the chimeric isoprenoid sesquiterpene synthase polypeptide encoded by the DNA catalyzes the production of at least one isoprenoid sesquiterpene synthase reaction product that is not produced in the absence of the second ...

AGENT FOR REDUCING ACETALDEHYDE IN ORAL CAVITY

Disclosed herein is a novel enzymatic agent effective in reducing acetaldehyde in the oral cavity. It has been found that an aldehyde dehydrogenase derived from a microorganism belonging to the genus and a threonine aldolase derived from are effective in reducing low concentrations of acetaldehyde. Therefore, an agent for reducing acetaldehyde in the oral cavity is provided, which contains these enzymes as active ingredients. 1. An agent for reducing acetaldehyde in an oral cavity , comprising an aldehyde dehydrogenase or a threonine aldolase.2Saccharomyces.. The agent for reducing acetaldehyde in an oral cavity according to claim 1 , wherein the aldehyde dehydrogenase is derived from a microorganism belonging to the genus3SaccharomycesSaccharomyces cerevisiae.. The agent for reducing acetaldehyde in an oral cavity according to claim 2 , wherein the microorganism belonging to the genus is4Escherichia coli.. The agent for reducing acetaldehyde in an oral cavity according to claim 1 , wherein the threonine aldolase is derived from5. The agent for reducing acetaldehyde in an oral cavity according to claim 1 , which exhibits degradation activity against acetaldehyde at a substrate concentration of 1 μM to 1 mM.6. The agent for reducing acetaldehyde in an oral cavity according to claim 1 , which exhibits degradation activity against acetaldehyde at a substrate concentration of 1 μM to 100 μM.7. An oral composition comprising the agent for reducing acetaldehyde in an oral cavity according to .8. A method for reducing acetaldehyde in saliva claim 7 , comprising allowing the oral composition according to to act on saliva.9. The method according to claim 8 , which is effective in reducing oral odor.10. The method according to claim 8 , which is effective in preventing cancer whose cause or one of causes is acetaldehyde. The present invention relates to an agent for reducing acetaldehyde in the oral cavity. More specifically, the present invention relates to an agent that ...

Methods and Compositions for Treating Oxalate-Related Conditions

The subject invention relates in one aspect to an oxalate degrading composition, which includes at least one oxalate degrading enzyme. The composition includes an enriched insoluble component of fungal biosample, and the composition is effective to degrade oxalate at a pH of 1.9 or higher. The composition is protected from protease degradation such as pepsin, trypsin and chymotrypsin. The composition is capable of withstanding the conditions of the stomach, small intestines, and/or large intestines of a subject. 1. An oxalate degrading composition , said composition comprising:at least one oxalate degrading enzyme, said composition comprising an enriched insoluble component of a fungal biosample, and wherein said composition is effective to degrade oxalate at a pH of 1.9 or higher.2. The composition of claim 1 , wherein said at least one oxalate degrading enzyme comprises a first enzyme that is active at a pH within a pH range of 1.9-6.3 and/or a second enzyme that is active at a pH within a pH range of 5.0-8.0 claim 1 , or a combination of said first and second enzymes.3. The composition of claim 1 , wherein said at least one oxalate degrading enzyme comprises at least one of oxalate-oxidase (OxOx) claim 1 , and/or oxalate decarboxylase (OxDC).4Dentinum reparandum, Russula virescens, Armillaria tabescens, Cantharellur cinnabarinur, Boletur rubellusCollybia acervata, Crepidotus mollis, Boletur subglabripes, Boletus ornatipes, Polyporus elegans, Pluteus cervinus, Sderoderma citrinum, Pleurotus ostreatus, Xerula radicata, Telephoro vlalis, Clitocybe, Cortinarius cedretorun, Lactarius indigo, Russula densifolia, Amanita rhopalopus, Clitocybe hydrograma, Amanita gemmata, Cortinarius lewisii, Pleurotus eryngii, Inocybe rimosa, Lactarius atrorividus, Russula cyanoxhanth, Sderoderma polyrhizum, Lentinula edodes, Hypsizygus tessellates, Flammulina velutipes, Leucangia carthusiana, Tuber oregonese, Grifola frondosa, Boletus rubricitrinus, Boletus fraternus, Gyroporus ...

ISOLATED HIGH AFFINITY ENTITIES WITH T-CELL RECEPTOR LIKE SPECIFICITY TOWARDS NATIVE COMPLEXES OF MHC CLASS II AND GLUTAMIC ACID DECARBOXYLASE (GAD) AUTOANTIGENIC PEPTIDES

Provided are isolated complexes comprising a major histocompatibility complex (MHC) class II and a type I diabetes-associated GAD autoantigenic peptide, the isolated complex having a structural conformation which enables isolation of a high affinity entity which comprises an antigen binding domain capable of specifically binding to a native conformation of a complex composed of the MHC class II and the type I diabetes-associated GAD autoantigenic peptide; and isolated high affinity entities comprising an antigen binding domain capable of specifically binding the complex, wherein the isolated high affinity entity does not bind to the MHC class II in an absence of the diabetes-associated GAD autoantigenic peptide, wherein the isolated high affinity entity does not bind to the diabetes-associated GAD autoantigenic peptide in an absence of the MHC class II; and methods and kits using same for diagnostic and therapeutic purposes. 1. An isolated complex comprising a major histocompatibility complex (MHC) class II and a Glutamic acid decarboxylase (GAD) autoantigenic peptide , wherein said GAD autoantigenic peptide comprises a core amino acid sequence set forth by SEQ ID NO:14 (GAD556-565 , FFRMVISNPA) , wherein said GAD autoantigenic peptide is covalently attached to a beta chain of said MHC class II.2. The isolated complex of claim 1 , wherein said GAD autoantigenic peptide is covalently bound at a C terminus thereof to an N-terminus of an extracellular domain of a beta chain of said MHC class II.3. The isolated complex of claim 1 , wherein said GAD autoantigenic peptide is covalently embedded between amino acids 1-6 of an extracellular domain of a beta chain of said MHC class II.4. The isolated complex of claim 1 , wherein said GAD autoantigenic peptide is covalently attached to said beta chain between the third and forth amino acid of a mature polypeptide of said MHC class II beta chain.5. An isolated antibody comprising an antigen binding domain capable of ...

Acellular Bioabsorbable Tissue Regeneration Matrices

The present invention provides methods and compositions useful in the regeneration of damaged, lost and/or degenerated tissue in humans and animals. In certain embodiments, the present invention provides an acellular bioabsorbable tissue regeneration matrix, methods of making such a matrix, and methods of using such a matrix for the regeneration of damaged, lost and/or degenerated tissue. In certain embodiments, methods and compositions of the present invention are useful in the treatment of damaged, lost and/or degenerated nerve tissue. 178-. (canceled)79. An isolated acellular bioabsorbable tissue regeneration matrix comprising: a proteinaceous core having a protein content of at least 1%; wherein the structure of the acellular bioabsorbable tissue regeneration matrix is characterized by spherical bodies with a diameter of approximately at least 100 nm; and further wherein the acellular bioabsorbable tissue regeneration matrix lacks substantial metabolic activity; and further wherein the acellular bioabsorbable tissue regeneration matrix is capable of initiating more tissue regeneration in a subject with tissue damage , increasing tissue regeneration in a subject with tissue damage , or both.80. The isolated acellular bioabsorbable tissue regeneration matrix of claim 79 , further comprising one or more proteins selected from the group consisting of:transferrin, serum albumin, serum albumin precursor, complement component 3, chains A-D hemoglobin, IgM, IgG1, medullasin inhibitor 2, carbonic anhydrase, CA1 protein, and combinations thereof.81. The isolated acellular bioabsorbable tissue regeneration matrix of claim 79 , wherein the spherical bodies are recognized by CD56 antibodies.82. The acellular bioabsorbable tissue regeneration matrix of claim 79 , wherein the spherical bodies have a diameter of about 1-2 μm.83. The acellular bioabsorbable tissue regeneration matrix of claim 79 , wherein the spherical bodies have a diameter of about 2-4 μm.84. The acellular ...

PRODUCTION OF MONOTERPENES

The present invention relates to methods for producing monoterpenes, particularly tricyclene, by culturing microbial organisms that express a terpene synthase and optionally a prenyl transferase. 1. A method for producing tricyclene comprising:culturing a microbial organism expressing a heterologous terpene synthase under conditions in which the terpene synthase converts geranyl diphosphate to tricyclene, wherein the tricyclene is produced at a level of at least 0.5% of total monoterpene production by the organism.2. The method according to claim 1 , wherein the terpene synthase is a bornyl diphosphate synthase or a variant thereof.3. The method according to claim 1 , wherein the terpene synthase has at least 80% sequence identity to SEQ ID NO: 2 or 4.4. (canceled)5. The method according to claim 2 , wherein the terpene synthase comprises at least 90% sequence identity to SEQ ID NO: 2 claim 2 , and comprises an amino acid substitution at one or both of positions V399 and I404 of SEQ ID NO: 2.6. The method according to claim 5 , wherein the substitution at position V399 is V399I.7. The method according to claim 5 , wherein the terpene synthase further comprises an amino acid substitution at one or more of positions S4 claim 5 , E159 claim 5 , G338 claim 5 , S267 claim 5 , I291 claim 5 , I297 claim 5 , K285 claim 5 , T460 claim 5 , and F525 of SEQ ID NO: 2.8. The method according to claim 1 , wherein the terpene synthase is a camphene synthase or a variant thereof.9. The method according to claim 8 , wherein the terpene synthase has at least 80% sequence identity to SEQ ID NO: 6 or 8.10. (canceled)11. The method according to claim 8 , wherein the terpene synthase comprises at least 90% sequence identity with SEQ ID NO: 6 claim 8 , and comprises an amino acid substitution at one or more of positions N18 claim 8 , A283 claim 8 , I320 claim 8 , and T431 of SEQ ID NO: 6.12. The method according to claim 11 , wherein the terpene synthase further comprises an amino acid ...

(r)-hydroxynitrile lyase from brassicaceae

The invention concerns a polypeptide which can be isolated from the Brassicaceae family and which has at least the activity of a hydroxynitrile lyase (HNL). The hydroxynitrile lyase of the invention is the first HNL from the Brassicaceae family. The plants ( Arabidopsis ) from which this enzyme or its gene is isolated is also described as non-cyanogenic. All HNL-containing plants described so far are cyanogenic plants and so it has until now been assumed that only cyanogenic plants contain hydroxynitrile lyases. Surprisingly, it transpires that a polypeptide (AtHNL) of the invention is (R)-selective. The amino acid sequence gives a theoretical molecular weight of 29.2 kDa for the AtHNL subunit. The calculated molecular mass of the protein of approximately 30 kDa can be confirmed by SDS gel electrophoresis.

Heat-Stable Persephonella Carbonic Anhydrases and Their Use

The present invention relates to use of Persephonella carbonic anhydrase in CO 2 extraction, e.g., from flue gas, natural gas, biogas or ambient air. The Persephonella carbonic anhydrases are especially well suited for these purpose due to their extreme thermostability.

NOVEL ALDOLASE AND PRODUCTION PROCESS OF SUBSTITUTED ALPHA-KETO ACIDS

4-(Indol-3-ylmethyl)-4-hydroxy-2-oxoglutarate, which is useful as an intermediate in the synthesis of monatin, may be synthesized from indole pyruvic acid and pyruvic acid (and/or oxaloacetic acid) by using a novel aldolase derived from the genus or 1. An isolated polynucleotide of following (a) or (b):(e) a polynucleotide having the nucleotide sequence of SEQ ID NO: 15 or the nucleotide sequence of nucleotides 398 to 1141 of SEQ ID NO: 15; or(f) a polynucleotide that hybridizes under stringent conditions with a polynucleotide having the nucleotide sequence complementary to the full-length nucleotide sequence of SEQ ID NO: 15 or the nucleotide sequence of nucleotides 398 to 1141 of SEQ ID NO: 15, and encodes a protein having aldolase activity, wherein said stringent conditions comprise a wash step in 0.1×SSC and 0.1% SDS at 65° C.2. An isolated polynucleotide of following (c) or (d):(g) a polynucleotide that encodes a protein comprising the amino acid sequence of SEQ ID NO: 16; or(h) a polynucleotide that encodes a protein having an amino acid sequence that contains a substitution, deletion, insertion, or addition of one to ten amino acid residues in the amino acid sequence of SEQ ID NO: 16, and has aldolase activity.3. A recombinant DNA produced by ligating into a vector DNA a polynucleotide selected from the group consisting of:(e) a polynucleotide having the nucleotide sequence of SEQ ID NO: 15 or the nucleotide sequence of nucleotides 398 to 1141 of SEQ ID NO: 15;(f) a polynucleotide that hybridizes under stringent conditions with a polynucleotide having the nucleotide sequence complementary to the full-length nucleotide sequence of SEQ ID NO: 15 or the nucleotide sequence of nucleotides 398 to 1141 of SEQ ID NO: 15, and encodes a protein having aldolase activity, wherein said stringent conditions comprise a wash step in 0.1×SSC and 0.1% SDS at 65° C.;(g) a polynucleotide that encodes a protein comprising the amino acid sequence of SEQ ID NO: 16; and(h) a ...

POLYPEPTIDE HAVING DITERPENE SYNTHASE ACTIVITY

The present application, among others, relates to novel polypeptides having diterpene synthase activity, nucleic acid molecules encoding same, as well as to a gene cluster from which is thought to be involved in the biosynthetic pathway for producing pleuromutilin. 115.-. (canceled)16. An isolated polypeptide ,the polypeptide comprising an amino acid sequence which comprisesa sequence having at least 50% sequence identity to SEQ ID NO: 1,a sequence having at least 40% sequence identity to SEQ ID NO: 2, and i) a sequence having at least 15% sequence identity to SEQ ID NO: 7;', 'ii) a sequence having at least 25% sequence identity to SEQ ID NO: 4;', 'iii) a sequence having at least 45% sequence identity to SEQ ID NO: 5; and', 'iv) a sequence having at least 45% sequence identity to SEQ ID NO: 6,, 'at least one sequence selected from the group consisting of'}{'i': 'Clitopilus passeckerianus', 'wherein SEQ ID NOs: 1-2 and 4-7 are of origin and wherein said polypeptide is a diterpene synthase.'}17Clitopilus passeckerianus. The isolated polypeptide according to claim 16 , wherein said amino acid sequence further comprises a sequence having at least 50% sequence identity to SEQ ID NO: 3 claim 16 , wherein SEQ ID NO: 3 is of origin.18. The isolated polypeptide according to claim 16 , wherein the molecular weight of the polypeptide is between 90 kDa and 140 kDa.19. The isolated polypeptide according to claim 16 , wherein the polypeptide comprises an amino acid sequence which amino acid sequence comprises a sequence having at least 70% sequence identity to SEQ ID NO: 9.20. The isolated polypeptide according to claim 16 , wherein the polypeptide is capable of catalyzing the conversion of geranyl pyrophosphate into a pleuromutilin precursor.21. The isolated polypeptide according to claim 20 , wherein said pleuromutilin precursor is a compound according to formula (I).22. The isolated polypeptide according to claim 16 , wherein said polypeptide is derivable from a fungal host. ...

HIGHLY STABLE BETA-CLASS CARBONIC ANHYDRASES USEFUL IN CARBON CAPTURE SYSTEMS

The present disclosure relates to β-class carbonic anhydrase polypeptides having improved properties including increased thermostability and/or stability in the presence of amine compounds, ammonia, or carbonate ion. The present disclosure also provides formulations and uses of the polypeptides for accelerating the absorption of carbon dioxide from a gas stream into a solution as well as for the release of the absorbed carbon dioxide for further treatment and/or sequestering. Also provided are polynucleotides encoding the carbonic anhydrase polypeptides and host cells capable of expressing them. 149-. (canceled)50. A recombinant carbonic anhydrase polypeptide comprising an amino acid sequence having at least 80% identity to SEQ ID NO: 2 and comprising an amino acid residue difference relative to SEQ ID NO: 2 at a position selected from X30 , X40 , X84 , X96 , X120 , X121 , X139 , and X147.51. The recombinant carbonic anhydrase polypeptide of in which the amino acid residue difference at a position selected from X30 claim 50 , X40 claim 50 , X84 claim 50 , X96 claim 50 , X120 claim 50 , X121 claim 50 , X139 claim 50 , and X147 is selected from X30A claim 50 , X30K claim 50 , X30L claim 50 , X30Q claim 50 , X30R claim 50 , X40L claim 50 , X40Q claim 50 , X40W claim 50 , X84K claim 50 , X84N claim 50 , X84Q claim 50 , X84R claim 50 , X84S claim 50 , X96A claim 50 , X96C claim 50 , X96E claim 50 , X96K claim 50 , X120R claim 50 , X121H claim 50 , X121K claim 50 , X121L claim 50 , X121Q claim 50 , X121T claim 50 , X121V claim 50 , X121W claim 50 , X139H claim 50 , X139K claim 50 , X139M claim 50 , X139Q claim 50 , X147E claim 50 , X147F claim 50 , X147G claim 50 , and X147T.52. The recombinant carbonic anhydrase polypeptide of in which the amino acid residue difference at a position selected from X30 claim 50 , X40 claim 50 , X84 claim 50 , X96 claim 50 , X120 claim 50 , X121 claim 50 , X139 claim 50 , and X147 is selected from X30R claim 50 , X40L claim 50 , X84Q claim ...

MODIFIED ETHYLENEDIAMINE-N, N'-DISUCCINATE: ETHYLENEDIAMINE LYASE

The present invention provides a modified ethylenediamine-N,N′-disuccinate:ethylenediamine lyase. The present invention also provides a protein that comprises the amino acid sequence represented by SEQ ID NO: 1; or a protein that comprises an amino acid sequence derived from the amino acid sequence represented by SEQ ID NO: 1 by deletion, substitution, or addition of one or more amino acid residues, and has an ethylenediamine-N,N′-disuccinate:ethylenediamine lyase activity. 153-. (canceled)54. An isolated gene encoding a protein comprising the amino acid sequence of SEQ ID NO:1 and having an ethylenediamine-N ,N′-disuccinate:ethylenediamine lyase activity.55. An isolated gene encoding a protein comprising the amino acid sequence of SEQ ID NO:1 having 1 to 10 substitutions , and wherein the protein has ethylenediamine-N ,N′-disuccinate:ethylenediamine lyase activity that is heat resistant.56. The isolated gene of claim 55 , wherein one substitution is the substitution of the lysine residue at position 120 with a glutamic acid residue.56. The isolated gene of claim 55 , wherein one substitution is the substitution of the isoleucine residue at position 166 with a serine residue.58. The isolated gene of claim 55 , wherein one substitution is the substitution of the isoleucine residue at position 166 with a threonine residue.59. The isolated gene of claim 55 , wherein one substitution is the substitution of the alanine residue at position 365 with a valine residue.60. An isolated gene encoding a protein comprising the amino acid sequence of SEQ ID NO:1 having 2 to 10 substitutions claim 55 , wherein the substitutions include the substitution of the lysine residue at position 120 with a glutamic acid residue claim 55 , and wherein the protein has ethylenediamine-N claim 55 ,N′-disuccinate:ethylenediamine lyase activity that is heat resistant.61. The isolated gene of claim 60 , wherein the isoleucine residue at position 166 is substituted with a serine residue.62. The ...

SYSTEMS AND METHODS FOR BIOTRANSFORMATION OF CARBON DIOXIDE INTO HIGHER CARBON COMPOUNDS

Systems, compounds and methods for the conversion of C1 carbon compounds to higher carbon compounds useful for the generation of commodity compounds. 1. A method for converting formaldehyde to dihydroxyacetone , comprising contacting formaldehyde with a thiamine diphosphate cofactor and a polypeptide comprising a motif capable of associating with the thiamine diphosphate cofactor ,wherein the motif comprises a histidine residue in a first position, an asparagine or glutamine residue in a second position, and a glutamic acid or aspartic acid residue in a third position;wherein upon association with the thiamine diphosphate cofactor, the cofactor pyrimidine N1 is hydrogen bonded to the acid side chain of the glutamic acid residue or the acid side chain of the aspartic acid residue of the motif; andwherein the histidine N1 and the amide side chain of the asparagine residue or the amide side chain of the glutamine residue are capable of making a water-mediated hydrogen bond with the formaldehyde substrate and/or dihydroxyacetone product.2. The method of claim 1 , wherein the motif is incorporated in a benzaldehyde lyase polypeptide scaffold.3. The method of claim 2 , wherein the benzaldehyde lyase polypeptide scaffold comprises an amino acid sequence with at least 40% identity to the sequence set forth in SEQ ID NO:2 or SEQ ID NO:3.4. The method of claim 1 , wherein the polypeptide is engineered.5. The method of claim 4 , wherein the motif comprises at least one amino acid substitution corresponding to the substitutions selected from the group consisting of A394G claim 4 , A480W claim 4 , G419N claim 4 , A28S claim 4 , and A28I claim 4 , with reference to the amino acid sequence set forth in SEQ ID NO:2.6. The method of claim 5 , wherein the motif comprises the amino acid substitutions corresponding to A394G and A480W claim 5 , with reference to the amino acid sequence set forth in SEQ ID NO:2.7. The method of claim 4 , wherein the motif comprises at least three amino ...

HEAT-STABLE CARBONIC ANHYDRASES AND THEIR USE

The present invention relates to use of heat-stable carbonic anhydrase in COextraction, e.g., from flue gas, natural gas or biogas. Furthermore, the invention relates to isolated polypeptides having carbonic anhydrase activity at elevated temperatures and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides. 1Bacillus halodurans. A method of using a heat-stable carbonic anhydrase for extraction of carbon dioxide from a carbon dioxide-containing medium , comprising contacting a carbon dioxide-containing medium with a heat stable carbonic anhydrase that maintains activity at temperatures above 45° C. for at least 15 minutes , wherein the heat stable carbonic anhydrase is an alpha-carbonic anhydrase which is at least 85% identical to the alpha-carbonic anhydrase from (SEQ ID NO: 16) , wherein carbon dioxide is extracted from the carbon dioxide-containing medium.2Bacillus halodurans. The method in accordance with claim 1 , wherein the carbonic anhydrase is the alpha-carbonic anhydrase from (SEQ ID NO: 16).3. The method of claim 1 , where the carbonic anhydrase maintains activity at temperatures above 45° C. for at least two hours.4. The method of claim 1 , where the carbonic anhydrase is used in a bioreactor.5. The method of claim 4 , wherein the bioreactor comprises a contained liquid membrane.6. The method of claim 5 , wherein the membrane liquid of the contained liquid membrane contains a bicarbonate buffer with a pH of at least 9.0.7. The method of claim 1 , wherein the carbon dioxide-containing medium is a carbonic dioxide-containing gas.8. The method of claim 1 , wherein the carbon dioxide-containing medium is a multiphase mixture.9. The method of claim 7 , where the carbonic dioxide-containing gas is emitted from combustion or fermentation.10. The method of claim 7 , where the carbonic dioxide-containing gas is a flue gas.11. The method of claim 7 , where ...

Protoilludene synthase

The present invention relates to an isolated, recombinant or synthetic polynucleotide encoding a polypeptide with protoilludene synthase activity and comprising a sequence selected from the group consisting of a) SEQ ID Nos. 1 or 14 of the attached sequence listing; b) a nucleic acid sequence complementary to SEQ ID Nos. 1 or 14; c) nucleic acid sequences which hybridize under stringent conditions to the nucleic acid sequences defined in a) and b) or their complementary strands, as well as to the polypeptide encoded by the isolated polynucleotide, as well as a method for the production of melleolides employing the polynucleotide or polypeptide of the invention.

BACTERIOPHAGE-CONTAINING THERAPEUTIC AGENTS

The present invention relates in its broadest aspect to combined phage/antibiotic therapy. More particularly, it relates to use of (i) one or more bacteriophages and (ii) one or more antibiotics in the manufacture of a combined product for simultaneous, separate or sequential administration of (i) and (ii) to treat a bacterial infection characterized by biofilm formation, for example an infection comprising or consisting of . Treatment in this context may be either therapeutic or prophylactic treatment. Also provided are deposited bacteriophages each exhibiting different strain specificity against and combinations of such bacteriophages, e.g. a panel of six deposited bacteriophages which was found to be effective against a high percentage of clinical isolates of from canine ear infections. 135-. (canceled)36Pseudomonas aeruginosa. A panel of bacteriophages for treating a bacterial infection comprising , the panel comprising two or more bacteriophages selected from the group consisting of:(i) deposited strains NCIMB 41174, NCIMB 41175, NCIMB 41176, NCIMB 41177, NCIMB 41178, NCIMB 41179, NCIMB 41180, NCIMB 41181; and{'i': 'P. aeruginosa,', '(ii) mutants thereof that retain the ability to target'}wherein the mutant has at least 90% nucleotide sequence identity across its whole genome as compared to the genome of the deposited strain, and{'i': 'P. aeruginosa.', 'each member of the panel has a different strain specificity for'}37. The panel of claim 36 , wherein the mutant has at least 95% nucleotide sequence identity across its whole genome as compared to the genome of the deposited strain.38. The panel of claim 36 , wherein the mutant has at least 97% nucleotide sequence identity across its whole genome as compared to the genome of the deposited strain.39. The panel of claim 36 , wherein the mutant has at least 98% nucleotide sequence identity across its whole genome as compared to the genome of the deposited strain.40. The panel of claim 36 , wherein the mutant has at ...

Diterpene Synthases And Method For Producing Diterpenoids

Provided herein are diterpene synthases (diTPS) and methods for producing diterpenoids. Also provided herein are nucleic acid sequences encoding diTPS, diTPS amino acid sequences, diTPS proteins, vectors, cells, transgenic organisms, uses, compositions, methods, processes, and kits thereof. 1. An isolated nucleic acid molecule , comprising a sequence of nucleotides encoding a cis-abienol synthase (CAS) polypeptide selected from among:a) the polypeptide whose sequence is set forth in one of SEQ ID NOS:7, 50 and 55;b) an active fragment of the polypeptide of a); andc) a polypeptide having a sequence of amino acids that has at least 85% sequence identity with a polypeptide of a) or b),wherein the encoded polypeptide or active fragment catalyzes the formation of cis-abienol from geranylgeranyl diphosphate (GGPP).2. The isolated nucleic acid molecule of claim 1 , wherein the sequence of nucleotides encodes a polypeptide that comprises the sequence of amino acids set forth in one of SEQ ID NOS:7 claim 1 , 50 and 55 or an active fragment thereof.3. The isolated nucleic acid molecule of claim 1 , wherein the sequence of nucleotides encodes a polypeptide that consists of the sequence of amino acids set forth in one of SEQ ID NOS:7 claim 1 , 50 and 55 or an active fragment thereof.4. The isolated nucleic acid molecule of claim 1 , wherein the active fragment is a pseudomature form.5. The isolated nucleic acid molecule of claim 4 , wherein the sequence of nucleotides encodes a cis-abienol synthase (CAS) polypeptide whose sequence is set forth in SEQ ID NO:50 or 55 claim 4 , or encodes a polypeptide whose sequence has at least 85% sequence identity with SEQ ID NO:50 or 55.6. The isolated nucleic acid molecule of claim 1 , comprising a sequence of nucleotides selected from among:a) the nucleic acid molecule whose sequence is set forth in one of SEQ ID NOS:8, 54 and 56; andb) a nucleic acid molecule whose sequence of nucleotides has at least 85% sequence identity to the sequence ...

AGENT FOR NEUROPATHIC PAIN

An object of the present invention is to provide a substance which can be used as an active ingredient for improving neuropathic pain having a novel mechanism of action different from those of currently available agents and, therefore, provide an improving agent for neuropathic pain which rarely interacts with currently available agents and also does not have adverse reactions similar to those of currently available agents. An improving agent for neuropathic pain due to a hyperalgesic response of the present invention as a means for resolution is characterized by comprising, as an active ingredient, a lyase (an elimination enzyme) which has an activity of degrading a chondroitin sulfate chain of a chondroitin sulfate proteoglycan, and is typified by chondroitinase ABC which selectively removes chondroitin sulfate and dermatan sulfate of a proteoglycan. 15.-. (canceled)6. A method for treating neuropathic pain due to a hyperalgesic response , comprising the step of:administering to a patient having a neuropathic pain due to a hyperalgesic response, a lyase having an activity of degrading a chondroitin sulfate chain of a chondroitin sulfate proteoglycan.7. The method of claim 6 , wherein the lyase is chondroitinase ABC.8. The method of claim 6 , wherein the patient has allodynia.9. The method of claim 6 , wherein the neuropathic pain is caused by a central nervous disorder.10. The method of claim 6 , wherein the neuropathic pain is caused by a spinal cord injury.11. The method of claim 6 , wherein:the patient has a neuropathic pain caused by a nerve injury; andthe lyase is continuously administered to the site of the neuropathic pain.12. The method of claim 11 , wherein the lyase is administered intrathecally to the subarachnoid cavity.13. The method of claim 11 , wherein the lyase is continuously administered starting from immediately to 3 days after the injury claim 11 , for a period of up to 8 weeks.14. The method of claim 11 , wherein the step of administering the ...

ULVAN LYASE, METHOD FOR MANUFACTURING SAME, AND USES THEREOF

The present invention notably relates to ulvan lyases, to nucleic acid sequences coding for these ulvan lyases, to vectors comprising these coding sequences, to a method of manufacturing these ulvan lyases, as well as to a method of degrading ulvans using these ulvan lyases and applicable applications to the degradation products of the ulvans. The ulvan lyases of the present invention, or ulvanolytic protein, are notably defined as proteins of 30 or 46 kD comprising the following four sequences in their peptide sequence: PNDPNLK, LLEVGNTGTFGSTGS, DLANPDNV and WNLPE. 2. The ulvan lyase according to claim 1 , said protein being of sequence SEQ ID No. 1.3. The ulvan lyase according to claim 2 , further comprising sequence SEQ ID No. 2 at its C-terminal end.4. The ulvan lyase according to claim 1 , further comprising a signal sequence at its N-terminal end.5. The ulvan lyase according to claim 4 , wherein the signal sequence is sequence SEQ ID No. 3.6. Nucleic acid of sequence SEQ ID No. 5.7. The nucleic acid according to claim 6 , further comprising sequence SEQ ID No. 6 at its 3′ end.8. The nucleic acid according to claim 6 , further comprising sequence SEQ ID No. 7 at its 5′ end.9. A vector comprising a nucleic acid claim 6 , the nucleic acid chosen sequence from SEQ ID No. 5 claim 6 , sequence SEQ ID No. 5 having sequence SEQ ID No. 6 at its 3′ end claim 6 , sequence ID No. 5 having sequence SEQ ID No. 7 at its 5′ end claim 6 , and sequence SEQ ID No. 5 having sequence SEQ ID No. 6 at its 3′ end and sequence SEQ ID No. 7 at its 5′ end.10. A host cell comprising a nucleic acid sequence or a vector claim 6 , the nucleic acid chosen from sequence SEQ ID No. 5 claim 6 , sequence SEQ ID No. 5 having sequence SEQ ID No. 6 at its 3′ end claim 6 , sequence ID No. 5 having sequence SEQ ID No. 7 at its 5′ end claim 6 , and sequence SEQ ID No. 5 having sequence SEQ ID No. 6 at its 3′ end and sequence SEQ ID No. 7 at its 5′ end claim 6 , and the vector comprising any of the ...

LEUCINE BETA ROLL DOMAINS AND USES THEREOF

In one aspect, the invention relates to a peptide that forms a calcium-dependent hydrogel using a rationally engineered beta roll peptide. In the absence of calcium, the peptide is intrinsically disordered. Upon addition of calcium, the peptide forms a corkscrew-like structure. In one embodiment, one face of the beta roll is mutated to comprise leucine residues. In some embodiments, a leucine zipper forming helical domain to the engineered beta roll forms hydrogels by physical cross-linking in calcium rich environments. 1. A beta roll comprising a scaffold from the RTX domain of adenylate cyclase , wherein leucine mutations are introduced on the beta roll domain.2. The beta roll of claim 1 , wherein the beta roll domain comprises the amino acid sequence XXXXXXXXX(SEQ ID NO: 10) claim 1 , wherein{'sub': '1', '(a) Xis an amino acid selected from the group consisting of glycine, valine and serine;'}{'sub': '2', '(b) Xis an amino acid selected from the group consisting of glycine, serine, aspartic acid and leucine;'}{'sub': '3', '(c) Xis an amino acid selected from the group consisting of alanine, glutamic acid, glutamine, tyrosine and glycine;'}{'sub': '4', '(d) Xis an amino acid selected from the group consisting of glycine and arginine;'}{'sub': '5', '(e) Xis an amino acid selected from the group consisting of aspartic acid, alanine, asparagine, serine, and histidine;'}{'sub': '6', '(f) Xis an amino acid selected from the group consisting of aspartic acid and asparagine;'}{'sub': '7', '(g) Xis an amino acid selected from the group consisting of valine, leucine, and threonine;'}{'sub': '8', '(h) Xis an amino acid selected from the group consisting of leucine, isoleucine, and tyrosine; and'}{'sub': '9', '(i) Xis an amino acid selected from the group consisting of isoleucine, leucine, serine, and arginine.'}3. The beta roll of claim 2 , wherein the beta roll domain further comprises X claim 2 , wherein Xis appended adjacent to X claim 2 , and wherein{'sub': '10', '(a) ...

Method for biocatalytic production of nitriles from oximes and oxime dehydratases usable therein

The present invention relates to novel methods for biocatalytic production of nitriles from oximes using oxime dehydratases and novel mutants with oxime dehydratase activity and use thereof in a process for biocatalytic production of nitriles, such as in particular for the production of citral nitrile, neral nitrile, geranial nitrile or citronellyl nitrile from citral oxime, neral oxime, geranial oxime or citronellal oxime; and oxime dehydratases usable therefor, nucleotide sequences therefor and expression constructs or microorganisms comprising these.

SOLVENT AND METHOD FOR CO2 CAPTURE FROM FLUE GAS

The present disclosure describes the efficient use of a catalyst, an enzyme for example, to provide suitable real cyclic capacity to a solvent otherwise limited by its ability to absorb and maintain a high concentration of COcaptured from flue gas. This invention can apply to non-promoted as well as promoted solvents and to solvents with a broad range of enthalpy of reaction. 1. A solvent solution for the capture of COfrom a flue gas stream , the solvent solution including:an amine solvent; and{'sub': '2', 'a catalyst achieving increased COloadings in the amine solvent as compared to a non-catalyzed solvent at temperatures in the range of 80-140° F.'}2. The solvent solution of claim 1 , wherein the catalyst is a biocatalyst.3. The solvent solution of claim 1 , wherein the biocatalyst is carbonic anhydrase or an analog thereof.4. The solvent solution of claim 1 , wherein the amine solvent has a theoretical cyclic capacity greater than or equal to about 1 mole/liter.5. The solvent solution of claim 1 , wherein the amine solvent has an acid dissociation constant (pKa) greater than or equal to about 9 and less than or equal to about 10.5.6. The solvent solution of claim 1 , wherein the amine solvent is selected from the group including DMEA (dimethylethanolamine) claim 1 , DEEA (diethylethanolamine) claim 1 , and DMgly (dimethylglycine).7. A method of reducing energy demand of a system for capturing COfrom a flue gas stream using an amine solvent claim 1 , the method comprising:{'sub': 2', '2', '2', '2, 'claim-text': an amine solvent, and', {'sub': '2', 'a catalyst achieving increased COloadings in the amine solvent as compared to a non-catalyzed solvent at temperatures in the range of 80-140° F.; and'}], 'applying a COlean solvent solution to a COrich flue gas stream in an absorber column to provide a COrich solvent solution and a COlean flue gas stream, the solvent solution including{'sub': 2', '2, 'reducing a temperature of the COlean solvent solution provided to the ...

Purification of Cystathionine Beta-Synthase

This invention provides chromatographic methods for the purification of a cystathionine β-Synthase (CBS) protein, particularly truncated variants thereof and compositions and pharmaceutical compositions prepared therefrom. 1. A method for purifying cystathionine β-Synthase (CBS) protein , wherein the CBS protein is a naturally occurring , chemically cleaved or genetically engineered truncated CBS protein , comprising the steps of:(a) providing a CBS-containing solution comprising one or a plurality of impurities; and(b) performing chromatographic separation of the CBS-containing solution using an ion exchange chromatography column and a metal affinity chromatography (IMAC) resin, wherein the impurities are removed thereby.2. The method of claim 1 , further comprising the step of performing chromatographic separation using a Hydrophobic Interaction Chromatography (HIC) column.3. The method of claim 1 , further comprising the step of performing chromatographic separation using a ceramic hydroxyapaptite resin.4. The method of claim 1 , wherein the ion exchange chromatography column is a weak anion exchanger.5. The method of claim 4 , wherein the weak anion exchanger is a DEAE-Sepharose FF column.6. The method of claim 1 , wherein the metal affinity chromatography (IMAC) resin is charged with a divalent metal cation.7. The method of claim 6 , wherein the divalent metal cation is nickel claim 6 , copper claim 6 , cobalt or zinc.8. The method of claim 7 , wherein the divalent metal ion is zinc.9. The method of claim 1 , further comprising eluting CBS from the metal affinity chromatography (IMAC) resin with an elution buffer comprising imidazole.10. The method of claim 1 , wherein the truncated CBS protein has an amino acid sequence identified by SEQ ID NO: 3.11. The method of claim 1 , wherein the CBS-containing solution is a clarified CBS solution.12. The method of claim 1 , wherein the CBS is produced in a recombinant cell.13. The method of claim 12 , wherein the ...

Three-dimensional structure of isoprene synthase and its use thereof for generating variants

The present invention provides a three-dimensional structures of P. tremuloides isoprene synthase and P. alba isoprene synthase. The invention also provides methods of using the three-dimensional structure to design isoprene synthases with improved activity for increased isoprene production in microbial host cells. Biosynthetically produced isoprene of the present invention finds use in the manufacture of rubber and elastomers.

NOVEL ALDOLASE AND PRODUCTION PROCESS OF SUBSTITUTED ALPHA-KETO ACIDS

4-(Indol-3-ylmethyl)-4-hydroxy-2-oxoglutarate, which is useful as an intermediate in the synthesis of monatin, may be synthesized from indole pyruvic acid and pyruvic acid (and/or oxaloacetic acid) by using a novel aldolase derived from the genus , or 1. An isolated polynucleotide of following (a) or (b):(e) a polynucleotide having the nucleotide sequence of SEQ ID NO: 15 or the nucleotide sequence of nucleotides 398 to 1141 of SEQ ID NO: 15; or(f) a polynucleotide that hybridizes under stringent conditions with a polynucleotide having the nucleotide sequence complementary to the full-length nucleotide sequence of SEQ ID NO: 15 or the nucleotide sequence of nucleotides 398 to 1141 of SEQ ID NO: 15, and encodes a protein having aldolase activity, wherein said stringent conditions comprise a wash step in 0.1×SSC and 0.1% SDS at 65° C.2. An isolated polynucleotide of following (c) or (d):(g) a polynucleotide that encodes a protein comprising the amino acid sequence of SEQ ID NO: 16; or(h) a polynucleotide that encodes a protein having an amino acid sequence that contains a substitution, deletion, insertion, or addition of one to ten amino acid residues in the amino acid sequence of SEQ ID NO: 16, and has aldolase activity.3. A recombinant DNA produced by ligating into a vector DNA a polynucleotide selected from the group consisting of:(e) a polynucleotide having the nucleotide sequence of SEQ ID NO: 15 or the nucleotide sequence of nucleotides 398 to 1141 of SEQ ID NO: 15;(f) a polynucleotide that hybridizes under stringent conditions with a polynucleotide having the nucleotide sequence complementary to the full-length nucleotide sequence of SEQ ID NO: 15 or the nucleotide sequence of nucleotides 398 to 1141 of SEQ ID NO: 15, and encodes a protein having aldolase activity, wherein said stringent conditions comprise a wash step in 0.1×SSC and 0.1% SDS at 65° C.;(g) a polynucleotide that encodes a protein comprising the amino acid sequence of SEQ ID NO: 16; and(h) a ...

ENZYME COMBINATIONS TO REDUCE BRAIN TISSUE SWELLING

Tissue fixed charge density (FCD) is identified as another potential therapeutic target for reducing brain tissue swelling. Reduction of the FCD could reduce the thermodynamic force driving water entry into the brain. The present invention discloses chondroitinase ABC (ChABC) reduces tissue FCD and reduces tissue swelling, indicating that it may be an effective treatment to reduce edema and control intracranial pressure. 1. A method of reducing brain tissue swelling , comprising the step of contacting the brain tissue with a composition comprising enzymes that reduce fixed charge density of the brain tissue.2. The method of claim 1 , wherein the enzymes digest chondroitin sulfate proteoglycans or heparin sulfate proteoglycans.3. The method of claim 2 , wherein the enzyme that digests chondroitin sulfate proteoglycans is chondroitinase ABC.4. The method of claim 2 , wherein the enzyme that digests heparin sulfate proteoglycans is heparinase.5. The method of claim 4 , wherein the heparinase is heparinase I and heparinase III.6. The method of claim 1 , wherein the composition further comprises enzyme that digests DNA.7. The method of claim 6 , wherein the enzyme that digests DNA is DNase I.8. A method of reducing brain tissue swelling in a subject claim 6 , comprising the step of administering to the subject a composition comprising enzymes that reduce fixed charge density of the brain tissue.9. The method of claim 8 , wherein the enzymes digest chondroitin sulfate proteoglycans or heparin sulfate proteoglycans.10. The method of claim 9 , wherein the enzyme that digests chondroitin sulfate proteoglycans is chondroitinase ABC.11. The method of claim 9 , wherein the enzyme that digests heparin sulfate proteoglycans is heparinase.12. The method of claim 11 , wherein the heparinase is heparinase I and heparinase III.13. The method of claim 8 , wherein the composition further comprises enzyme that digests DNA.14. The method of claim 13 , wherein the enzyme that digests DNA ...

USE OF PROKARYOTIC SPHINGOSINE-1-PHOSPHATE LYASES AND OF SPHINGOSINE-1-PHOSPHATE LYASES LACKING A TRANSMEMBRANE DOMAIN FOR TREATING HYPERPROLIFERATIVE AND OTHER DISEASES

The present invention relates to the use of prokaryotic sphingosine-1-phosphate lyases (S1PL) and S1PLs that lack a transmembrane domain or of a nucleic acid encoding such an S1PL in the prevention or treatment of a disease condition associated with elevated levels of sphingosine-1-phosphate (S1P), and for which S1P elevation is directly or indirectly causative. In addition, the invention relates to a new product in the form of S1PL lacking the N-terminal loop domain. 1. A transmembrane domain-free sphingosine-1-phosphate lyase (S1PL) or functional derivative or mutant thereof or a nucleic acid encoding a transmembrane domain-free S1PL or a functional derivative or mutant thereof for the prevention or treatment of a pathologic condition associated with elevated levels of sphingosine-1-phosphate (S1P).2. The transmembrane domain-free S1PL or nucleic acid of wherein the S1PL or a nucleic acid coding therefore is derived from a bacterium or an amoeba.3Symbiobacterium thermophilum, Erythrobacter litoralis, Myxococcus xanthus, Burkholderia thailandensis, Burkholderia pseudomallei, ErythrobacterMyxococcus fulvus, StreptomycesStigmatella aurantiaca, Rhodococcus erythropolis, Plesiocystis pacificaFluoribacter dumoffii.. The transmembrane domain-free S1PL or nucleic acid of wherein the bacterium is selected from the group consisting of sp. claim 2 , sp. claim 2 , and4. The transmembrane domain-free S1PL or nucleic acid of wherein the S1PL is selected from the group consisting of SEQ ID NO: 1 to 26 claim 1 , 28 and 36 or wherein the nucleic acid comprises a nucleotide sequence encoding an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to 26 claim 1 , 28 and 36.5Polysphondylium pallidum.. The transmembrane domain-free S1PL or nucleic acid of wherein the amoeba is6. The transmembrane domain-free S1PL or nucleic acid of wherein the S1PL has an amino acid sequence of SEQ ID NO: 27 or wherein the nucleic acid comprisies a nucleotide sequence coding for an ...

ISOPRENE SYNTHASE VARIANTS FOR IMPROVED MICROBIAL PRODUCTION OF ISOPRENE

The present invention provides methods and compositions comprising at least one isoprene synthase enzyme with improved catalytic activity and/or solubility. In particular, the present invention provides variant plant isoprene synthases for increased isoprene production in microbial host cells. Biosynthetically produced isoprene of the present invention finds use in the manufacture of rubber and elastomers. 156-. (canceled)57. An isolated host cell comprising a heterologous polynucleotide sequence encoding an isoprene synthase variant in operable combination with a promoter , wherein said isoprene synthase variant comprises one or more amino acid substitution(s) at one or more amino acid residues corresponding to a poplar isoprene synthase having the sequence of SEQ ID NO: 120 , wherein said substitution(s) are selected from the group consisting of V10M , F12S , T15A , E18G , V58I , V58F , L70Q , L70R , L70V , L70T , T71P , V79L , E89D , G94A , S119F , F120L , G127R , E175V , T212I , S257A , R262G , A266G , F280L , N297K , F305L , L319M , E323K , A328T , D342E , A359T , K366N , E368D , L374M , S396T , V4185 , K438N , H440R , T442A , I449V , A469S , K500R , K505Q , G507S , S509N , F511Y , and N532K; andwherein the variant is capable of more effectively converting dimethylallyl diphosphate (DMAPP) to isoprene, as compared to an isoprene synthase variant without a substitution.58. The host cell of wherein at least one amino acid substitution is a L70R substitution.59. The host cell of wherein at least one amino acid substitution is a G507S substitution.60. The host cell of wherein the variant comprises one of more amino acid substitutions selected from the group consisting of G127R/F511Y claim 57 , L70Q/G94A/R262G/F305L claim 57 , F12S/T15A/E18G/N297K claim 57 , S396T/T442I claim 57 , V10M/E323K claim 57 , F120L/A266G claim 57 , K438N/K500R claim 57 , V79L/S509N claim 57 , E175V/S257A/E368D/A469S claim 57 , T71P/L374M claim 57 , F280L/H440R claim 57 , E89D/H440R claim ...

ENZYMES THAT SYNTHESIZE ZINGIBERENE

The invention relates to nucleic acids encoding a zingiberene synthase that enables host cells and plants to make zingiberene that is useful in fragrances and for repelling or killing insects. The invention also relates to isolated zingiberene synthases and to methods for making zingiberenes. 1. An isolated nucleic acid encoding a zingiberene synthase with at least 95% sequence identity to amino acid SEQ ID NO: 2 , 4 , 6 , 8 , 11 , 12 , 14 , 16 , 18 , or a combination thereof.2. The isolated nucleic acid of claim 1 , wherein the nucleic acid comprises a sequence with at least 86% sequence identity to any of nucleotide sequences SEQ ID NO:1 claim 1 , 3 claim 1 , 5 claim 1 , 7 claim 1 , 13 claim 1 , 15 claim 1 , 17 claim 1 , 19 claim 1 , or a combination thereof.3. An expression cassette comprising the nucleic acid of operably linked to a promoter functional in a host cell.4. A host cell comprising the nucleic acid of .5. The host cell of claim 4 , further comprising a promoter operably linked to the nucleic acid claim 4 , wherein the promoter is functional in the host cell.6. The host cell of claim 5 , wherein the host cell is a plant cell.7. The host cell of claim 5 , wherein the host cell is a microorganism.8. A plant tissue comprising the nucleic acid of .9. A plant tissue comprising the host cell of .10. A plant comprising the nucleic acid of .11. A plant comprising the plant tissue of .12. A method of making a zingiberene comprising:{'claim-ref': {'@idref': 'CLM-00004', 'claim 4'}, 'a) culturing the host cell of under conditions sufficient for expression of the zingiberene synthase; and'}b) providing the host cell with a substrate for the zingiberene synthase to make the sesquiterpene.13. The method of claim 12 , wherein the substrate is 2Z claim 12 ,6Z-farnesyl diphosphate.14. The method of claim 12 , wherein the host cell is a bacterial or yeast cell.15E. coli. The method of claim 14 , wherein the bacterial cell is an cell.16. An isolated zingiberene synthase ...

COMPOSITION FOR PREVENTING OR TREATING OBESITY

Provided is a composition for preventing or treating obesity, and more particularly, a composition for preventing or treating obesity in order to treat or improve states of obese patients requiring weight control. The composition according to the present invention has advantages in that side effects by administration of the composition are not generated, and effects of losing weight and maintaining weight are excellent without changing food intake and consumption amounts, such that the composition may be effectively used to prevent overweight and obesity related diseases. 1. A composition for preventing or treating obesity , the composition comprising:a laptin based polypeptide, which is leptin, leptin derivatives, or a mixture thereof;an adenosine 5′-monophosphate-activated protein kinase (AMPK) activator; andinsulin, as active ingredients.2. The composition of claim 1 , wherein it comprises 1 to 300 ng/ml of the leptin based polypeptide claim 1 , 1 to 200 μg/ml of the AMPK activator claim 1 , and 0.1 to 30 ng/ml of insulin as the active ingredients.3. The composition of claim 2 , wherein it comprises to 250 ng/ml of the leptin based polypeptide claim 2 , 50 to 150 μg/ml of the AMPK activator claim 2 , and 1 to 15 ng/ml of insulin as the active ingredients.4. The composition of claim 1 , wherein the AMPK activator is acetyl-CoA carboxylase claim 1 , malonyl-CoA decarboxylase claim 1 , or a mixture thereof.5. The composition of claim 4 , wherein the AMPK activator is at least one selected from adiponectin claim 4 , metformin claim 4 , phenformin claim 4 , buformin claim 4 , thienopyridone claim 4 , 5′-aminoimidazole-4-carboxamide ribonucleoside (AICAR) claim 4 , resveratrol claim 4 , nootkatone claim 4 , and thiazoles.6. The composition of claim 1 , further comprising pharmaceutically acceptable salts.7. The composition of claim 1 , wherein the obesity means that a body mass index (BMI) is more than 25.8. A health food for preventing or treating obesity claim 1 , ...

ISOPRENE SYNTHASE VARIANTS WITH IMPROVED SOLUBILITY FOR PRODUCTION OF ISOPRENE

The present invention provides methods and compositions of variant polypeptides having isoprene synthase activity with improved solubility. In particular, the present invention provides isoprene synthase variant for increased isoprene production in recombinant host cells.

Method for Modifying a Property of a Protein

A method for improving the thermostability of a protein includes introducing, into the protein, two or more amino acid substitutions selected from the group consisting of: (i) substitution of an arginine residue for a lysine residue, (ii) substitution of a threonine residue for a serine residue, and (iii) substitution of an alanine residue for a serine residue. 1. A method for improving thermostability of a protein , the method comprising introducing , into said protein , two or more amino acid substitutions selected from the group consisting of:(i) substitution of an arginine residue for a lysine residue,(ii) substitution of a threonine residue for a serine residue, and(iii) substitution of an alanine residue for a serine residue.2. The method according to claim 1 , wherein said protein is a coryneform bacterium protein.3Corynebacterium glutamicum. The method according to claim 2 , wherein said protein is a protein.4. A method for producing a protein having a modified thermostability claim 2 , the method comprising: (i) substitution of an arginine residue for a lysine residue,', '(ii) substitution of a threonine residue for a serine residue, and', '(iii) substitution of an alanine residue for a serine residue; and, '(a) introducing two or more amino acid substitutions into a gene encoding a protein, wherein the two or more amino acid substitutions are selected from the group consisting of(b) introducing said gene obtained in (a) into a suitable host for gene expression to express the protein having the modified thermostability.5. The method according to claim 4 , wherein said protein is a coryneform bacterium protein.6Corynebacterium glutamicum. The method according to claim 5 , wherein said protein is a protein.7. A method for producing a microorganism having a modified thermostability claim 5 , the method comprising introducing two or more amino acid substitutions into a chromosomal DNA of a microorganism to modify a thermostability of the microorganism claim 5 , ...

Human Cystathionine Beta-Synthase Variants and Methods of Production Thereof

Human cystathionine β-synthase variants are disclosed, as well as a method to produce recombinant human cystathionine β-synthase and variants thereof. More particularly, the role of both the N-terminal and C-terminal regions of human CBS has been studied, and a variety of truncation mutants and modified CBS homologues are described. In addition, a method to express and purify recombinant human cystathionine β-synthase (CBS) and variants thereof which have only one or two additional amino acid residues at the N-terminus are described. 1. An isolated human cystathionine β-synthase (CBS) protein having CBS biological activity , said protein having: an amino acid sequence having an amino terminal deletion or a carboxyl terminal deletion or both an amino terminal and carboxyl terminal deletion and spanning from a starting position of one of amino acid residues from about 1-39 or 2-39 of SEQ ID NO: 2 to an ending position of one of amino acid residue 551 , or amino acid residue 413 , or an amino acid residue from about 397-551 or 414-551 of SEQ ID NO: 2; or a homologue thereof comprising an amino acid sequence that is at least about 70%-95% identical to said amino acid sequence , wherein said isolated human cystathionine β-synthase variant catalyzes the formation of cystathionine.28-. (canceled)9. The isolated human cystathionine β-synthase variant of claim 1 , wherein said ending position is amino acid residue 551 of SEQ ID NO: 2.10. The isolated human cystathionine β-synthase variant of claim 1 , wherein said ending position is amino acid residue 413 of SEQ ID NO: 2.11. The isolated human cystathionine β-synthase variant of claim 1 , wherein said ending position is one of amino acid residues from about 397-551 of SEQ ID NO: 2.12. The isolated human cystathionine β-synthase variant of claim 1 , wherein said ending position is one of amino acid residues from about 414-551 of SEQ ID NO: 2.1321-. (canceled)22. The isolated human cystathionine β-synthase protein of claim 1 , ...

MODIFIED 13-HYDROPEROXIDE LYASES AND USES THEREOF

Fatty acid 13-hydroperoxide lyase proteins which have been modified with respect to a previously described guava 13-hydroperoxide lyase and the nucleic acid sequences encoding these proteins. Also, recombinant nucleic acid molecules for expressing the modified 13-hydroperoxide lyases and methods of using such lyases in the field of organic synthesis. 125.-. (canceled)26. A modified 13-hydroperoxide lyase polypeptide comprising an amino acid sequence which has 1 to 40 amino acid alterations as compared to the amino acid sequence of the wild-type protein according to SEQ ID No. 1 and includes at least one amino acid alteration in a position selected from the group consisting of positions 3 , 4 , 5 , 19 , 208 , 340 , 342 , 352 , 354 , 358 , 359 , 360 , 371 , 372 , 375 , 377 , 382 , 383 , 387 , 388 , 389 , 392 , 393 , 394 , 395 , 399 and 457 of the amino acid sequence of the wild-type protein according to SEQ ID No. 1 , with the 13-hydroperoxide lyase having increased enzymatic activity as compared to the wild-type protein according to SEQ ID NO. 1.27. A method for preparing the modified 13-hydroperoxide lyase polypeptide of claim 26 , which comprises:culturing one or more transgenic cells comprising a recombinant nucleic acid molecule comprising a nucleotide sequence encoding a modified 13-hydroperoxide lyase comprising an amino acid sequence which has 1 to 40 amino acid alterations as compared to the amino acid sequence of the wild-type protein according to SEQ ID No. 1 and includes at least one amino acid alteration in a position selected from the group consisting of positions 3, 4, 5, 19, 208, 340, 342, 352, 354, 358, 359, 360, 371, 372, 375, 377, 382, 383, 387, 388, 389, 392, 393, 394, 395, 399 and 457 of the amino acid sequence of the wild-type protein according to SEQ ID No. 1, with the 13-hydroperoxide lyase having increased enzymatic activity as compared to the wild-type protein according to SEQ ID NO. 1, under conditions which permit expression of the ...

ENOLASE PEPTIDE CONJUGATE VACCINES AGAINST STAPHYLOCOCCUS AUREUS

The present invention relates to peptides of the enolase protein from as well as nucleic acid and nucleic acid sequence homologues encoding the peptides. The present invention also relates to a composition, particularly a vaccine, comprising one or more of the enolase peptides described herein or a fragment, derivative or variant thereof capable of generating an immune response that induces a protective antibody response or opsonophagocytic activity of human neutrophils for . The present invention also encompasses methods of treating and/or reducing the likelihood of a infection by administering a composition of the invention. 1. An isolated peptide consisting of a sequence of amino acids selected from the group consisting of: SEQ ID NO: 1 , 2 , 5 and 6 , or a variant or derivative.2. The isolated peptide of claim 1 , wherein said peptide comprises a derivative of the amino acid sequence set forth in SEQ ID NO: 1 claim 1 , 2 claim 1 , 5 or 6.3. The isolated peptide of claim 1 , wherein said peptide comprises a variant of the amino acid sequence set forth in SEQ ID NO: 1 claim 1 , 2 claim 1 , 5 or 6.4. The isolated peptide of claim 2 , wherein said derivative comprises one or more additional regions or moieties covalently joined to said amino acid sequence claim 2 , wherein each region or moiety is independently selected from a region or moiety having at least one of the following properties: enhances the immune response claim 2 , facilitates purification claim 2 , or facilitates polypeptide stability.5. The isolated peptide of claim 4 , wherein said derivative consists of an amino acid sequence as set forth in SEQ ID NO:1 claim 4 , 2 claim 4 , 5 claim 4 , or 6 with an N-terminal methionine.6. The isolated peptide of claim 1 , wherein said peptide consists essentially of the amino acid sequence set forth in SEQ ID NO: 1 claim 1 , 2 claim 1 , 5 claim 1 , or 6.7S. aureus. A composition able to induce a protective immune response in a patient against infection ...

COMPOSITIONS AND METHODS FOR TREATING OR PREVENTING OXALATE-RELATED DISEASE

The present invention comprises methods and compositions for the reduction of oxalate in humans, animals and plants. For example, the invention provides methods and compositions for the delivery of one ore more oxalate-reducing enzymes to the intestinal tracts of persons and animals. The methods and compositions can be used in treating and preventing oxalate-related conditions. 122-. (canceled)23Oxalobacter formigenes,. A method for reducing systemic circulating oxalate in a subject in need thereof , comprising: administering to a human or animal an effective amount of a composition comprising viable bacterial cells of oxalate-reducing enzymes , or both , wherein the administering is effected more than one time per day continuously every day for a period of months or years.24. The method of claim 23 , wherein the method is effective to reduce serum levels of oxalate.25. The method of claim 23 , wherein the method is effective to reduce blood levels of oxalate.26. The method of claim 23 , wherein the subject is suffering from an oxalate-related condition.27. The method of claim 26 , wherein the oxalate-related condition is selected from the group consisting of hyperoxaluria claim 26 , primary hyperoxaluria claim 26 , idiopathic calcium oxalate kidney stone disease claim 26 , urolithiasis claim 26 , enteric hyperoxaluria claim 26 , vulvodynia claim 26 , and oxalosis associated with end-stage renal disease.28Oxalobacter formigenes.. The method of claim 23 , wherein the composition comprises viable bacterial cells of29. The method of claim 23 , wherein the composition comprises oxalate-reducing enzymes selected from the group consisting of oxalate oxidase claim 23 , oxalate decarboxylase claim 23 , oxalyl-CoA decarboxylase claim 23 , formyl-CoA transferase claim 23 , and combinations of any two or more thereof.30. The method of claim 29 , wherein the oxalate-reducing enzymes are produced recombinantly.31. The method of claim 23 , wherein the composition further ...

Terpene Synthases and Methods of Using the Same

Disclosed are isolated nucleic acid molecules from that encode a terpene synthase protein at least 80% identical to a protein encoded by the nucleic acid sequence according to any of SEQ ID NOs: 1-47 or a degenerate variant thereof or a functional fragment thereof. Isolated terpene synthase proteins from are also disclosed. Host cells transformed with the terpene synthase nucleic acids are also disclosed, for example cells of a single cell organism, such as bacteria and yeast, or multicellular organism, such as a plant. The host cells can be prokaryotic cells or eukaryotic cells. Transgenic plants, or any part thereof, stably transformed with terpene synthase nucleic acids are also disclosed In some examples the transgenic plant is a dicotyledon or a monocotyledon. A method is disclosed for producing a transgenic plant, as is a method for producing terpenes. 1. An isolated nucleic acid molecule , comprising a nucleic acid sequence that encodes a terpene synthase protein at least 80% identical to a protein encoded by the nucleic acid sequence according to any of SEQ ID NOs: 1-47 or a degenerate variant thereof or a functional fragment thereof.2. The isolated nucleic acid molecule of claim 1 , further comprising a promoter operably linked to the nucleic acid sequence that encodes the terpene synthase protein.3. The isolated nucleic acid molecule of claim 1 , wherein the isolated nucleic acid comprises the cDNA set forth as anyone of SEQ ID NOs: 1-47 claim 1 , or a degenerate variant thereof.4. A construct comprising isolated nucleic acid molecule of any one of .5. The construct of claim 4 , wherein the construct confers an agronomic trait to a plant in which it is expressed.6. The construct of claim 5 , wherein the agronomic trait comprises terpenoid production.7. An expression vector comprising the nucleic acid molecule of .8. A host cell transformed with the vector of .9. The host cell of claim 8 , where the cell comprises a prokaryotic cell or a eukaryotic cell.10. ...

CYAA-CARRIED POLYPEPTIDE(S) AND USE TO INDUCE BOTH THERAPEUTIC AND PROPHYLACTIC IMMUNE RESPONSES

The invention is directed to means, based on CyaA-carried polypeptide(s), for use in the immunotherapeutic treatment of first determined pathological condition(s) diagnosed in a mammalian host by eliciting a T cell immune response against a first group of epitopes contained in said polypeptide(s) and in the prophylaxis against second determined pathological condition(s) in the same mammalian host by eliciting a T cell memory immune response against a second group of epitopes contained in said polypeptide(s), said immune responses being obtained after administration of said vector-carried polypeptide(s) into said host, wherein said prophylaxis against second determined pathological condition(s) is not observed when said second group of epitopes is not contained in said administered vector-carried polypeptide(s). 1. Vector-carried polypeptide(s) , wherein said vector carrying the polypeptide(s) consists in a CyaA protein or a fragment thereof suitable to present said polypeptide(s) to the immune system in a mammalian host , for use (i) in the immunotherapeutic treatment of first determined pathological condition(s) diagnosed in said mammalian host by eliciting a T cell immune response against a first group of epitopes contained in said polypeptide(s) and (ii) in the prophylaxis against second determined pathological condition(s) in the same mammalian host by eliciting a T cell memory immune response against a second group of epitopes contained in said polypeptide(s) , said immune responses being obtained after administration of said vector-carried polypeptide(s) into said host , wherein said prophylaxis against second determined pathological condition(s) is not observed when said second group of epitopes is not contained in said administered vector-carried polypeptide(s).2. The vector-carried polypeptide according to claim 1 , for further use (iii) in the prevention against the re-occurrence of said first determined pathological condition(s) claim 1 , by eliciting a T ...

ALGINATE MICROPARTICLES AND METHODS OF USING THE SAME

By combining the anti-bacterial effects of silver sulfadiazine and silver nanoparticles with the absorption and slow-release capabilities of alginate, a product was created that can be used to heal and protect deep wounds. These microparticles can have a greater surface area to volume ratio. This, in turn, can permit the particles to have a larger area of exposure to bacterial colonies, thereby increasing antimicrobial activity. Additionally, engineered microparticles also may benefit from the ability to conform to the shape of the wound. 1. A composition comprising an alginate microparticle comprising silver , wherein said alginate microparticle has a mean diameter of less than 10 μm.2. The composition of wherein said alginate microparticle comprises an alginate lyase.3. The microparticle population of wherein said mean diameter is about 7 μm.4. The microparticle population of wherein said microparticle population is stable with regard to particle size and appearance after 2 weeks of storage at 4° C.5. A method of delivery of an antiseptic comprising providing a composition comprising a microparticle population; said microparticles comprising an alginate and silver; wherein said microparticle population has a mean diameter of less than 10 μm.6. The method of claim 5 , wherein said microparticles further comprise an antibiotic or bacteriostatic.7. The method of wherein said silver comprises silver sulfadiazine claim 5 , silver nano particles and/or colloidal silver.8. The method of wherein said composition provides sustained release of said silver from said alginate microparticle.9. The method of claim 6 , wherein said composition provides sustained release of said antibiotic.10. The method of wherein said sustained release continues for not less than 24 hours.11. The method of claim 5 , further comprising:contacting a wound or infection site of a subject in need thereof with said composition comprising the microparticle population.12. The method of claim 5 , ...

Activity of Fe-S Cluster Requiring Proteins

The present invention is related to a recombinant host cell, in particular a yeast cell, comprising a dihydroxy-acid dehydratase polypeptide. The invention is also related to a recombinant host cell having increased specific activity of the dihydroxy-acid dehydratase polypeptide as a result of increased expression of the polypeptide, modulation of the Fe—S cluster biosynthesis of the cell, or a combination thereof. The present invention also includes methods of using the host cells, as well as, methods for identifying polypeptides that increase the flux in an Fe—S cluster biosynthesis pathway in a host cell. 131-. (canceled)32. A method of increasing the activity of an Fe—S cluster requiring protein in a recombinant host cell , comprising:(a) providing a recombinant host cell comprising an Fe—S cluster requiring protein;(b) changing the expression or activity of a polypeptide affecting Fe—S cluster biosynthesis in the host cell; and(c) growing the host cell of (b) under conditions whereby the activity of the Fe—S cluster requiring protein is increased.3362-. (canceled)63. The method of claim 32 , wherein the increase in activity is an amount greater than 10%.64. The method of claim 32 , wherein the increase in activity is greater than 5-fold.65. The method of claim 32 , wherein the Fe—S cluster requiring protein has dihydroxy-acid dehydratase activity (DHAD).66. The method of claim 32 , wherein the recombinant host cell comprises at least one heterologous polynucleotide encoding a polypeptide having DHAD activity.67. The method of claim 66 , wherein the polypeptide having DHAD activity is expressed in the cytosol of the host cell.68. The method of claim 66 , wherein the at least one heterologous polynucleotide encoding a polypeptide having DHAD activity is expressed in multiple copies.69. The recombinant host cell of claim 66 , wherein the at least one heterologous polynucleotide encoding a polypeptide having DHAD activity is integrated at least once in the ...

ENZYME PRODRUG CANCER THERAPY SELECTIVELY TARGETED TO TUMOR VASCULATURE AND METHODS OF PRODUCTION AND USE THEREOF

Methods of treating cancer by targeting tumor vasculature using an enzyme prodrug cancer therapy treatment are provided. 1. A method of treating at least one of a cancer tumor and cancer cells wherein the cancer tumor/cancer cells is supplied by a tumor vasculature , comprising the step of:contacting at least one blood vessel supplying a tumor with a therapeutically effective amount of a conjugate, the conjugate comprising a ligand having an enzyme operatively attached thereto, wherein the ligand has the ability to specifically and stably bind to at least one of an external receptor and a binding site on an outer surface of a tumor vasculature endothelial cell, wherein the at least one of an external receptor and a binding site is specific to the tumor vasculature endothelial cell, and wherein the enzyme is able to convert a prodrug into an active drug, and whereby the conjugate is maintained on the outer surface of the tumor vasculature endothelial cell;contacting the at least one blood vessel having the conjugate maintained thereon with a therapeutically effective amount of a prodrug, the prodrug comprising a substrate for the enzyme of the conjugate whereby the prodrug is convertible into an active anticancer drug by the enzyme of the conjugate; andwhereby the prodrug comes into contact with the conjugate in close proximity to the tumor vasculature endothelial cell and is converted into an active anticancer drug by the enzyme of the conjugate, and wherein the active anticancer drug is carried across the artery wall and travels inside the tumor vasculature endothelial cell by diffusion and permeation flow and directly causes death of the tumor vasculature endothelial cell.2. The method of claim 1 , wherein:(a) the ligand of the conjugate is selected from the group consisting of annexin V; antibodies to a receptor or aminophospholipid that is uniquely expressed or overexpressed on a surface of a tumor vasculature endothelial cell; RGD-motif peptides; NGR-motif ...

Aldolases, Nucleic Acids Encoding Them and Methods for Making and Using Them

This invention relates to polypeptides having aldolase activity, including pyruvate activity such as, without limitation, HMG and/or KHG aldolase activity, polynucleotides encoding these polypeptides, and methods of making and using these polynucleotides and polypeptides. In some embodiments, the invention is directed to polypeptides having aldolase activity, including pyruvate activity such as, without limitation, HMG and/or KHG aldolase activity, including thermostable and thermotolerant activity, and polynucleotides encoding these enzymes, and making and using these polynucleotides and polypeptides. The polypeptides in accordance with the invention can be used in a variety of pharmaceutical, agricultural and industrial contexts. In some embodiments, the invention provides polypeptides and biosynthetic pathways that are useful in the production of R-2-hydroxy 2-(indol-3ylmethyl)-4-keto glutaric acid (R-MP) and certain stereoisomers of monatin, such as R,R and S,R monatin, and salts thereof, as well as certain stereoisomers of monatin derivatives, such as the R,R and S,R configurations, and salts thereof. 1. An isolated , synthetic , or recombinant nucleic acid that encodes a polypeptide having aldolase activity , wherein the nucleic acid is selected from the group consisting of:(a) a variant nucleic acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or more or complete (100%) sequence identity to the full length of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:71, SEQ ID ...

PHARMACEUTICAL COMPOSITOIN FOR TREATING DEPRESSION AND METHOD FOR PREPARATION THEREOF

A pharmaceutical composition for treating depression and method for preparation thereof is provided. The pharmaceutical composition includes Radix Radix Glycyrrhizae, and/or their aqueous or alcoholic extract. Fructus Jujubae or their aqueous or alcoholic extract can also be included in the pharmaceutical composition. 1. A method for treating a depression of a patient , the method comprising a step of administering to the patient a pharmaceutical composition , wherein the pharmaceutical composition comprises:{'i': ginseng', 'ginseng, 'a extract extracted from 0.6˜400 parts by weight of a and having 0.5˜400% content of a ginsenoside; and'}0.16˜78.4 part by weight of a glycyrrhizically related acid.2ginsengginsengginseng. The method according to claim 1 , wherein the is one of a water extract and a ethanol extract claim 1 , and the glycyrrhizically related acid is one of a glycyrrhizic acid and a glycyrrhizic acid.3ginseng. The method according to claim 2 , wherein the ethanol extract comprises 20˜40% content of the ginsenoside claim 2 , and the purity of the glycyrrhizically related acid is 80˜98%.4. The method according to claim 1 , wherein the pharmaceutical composition further comprising a jujuba extract extracted from 0.00025˜0.6 part by weight of a jujuba and having 0.17˜100% content of a jujuba cyclic adenosine monophosphate (cAMP).5. The method according to claim 4 , wherein the jujuba ethanol extract comprises 0.5˜3% content of the jujuba cAMP.6ginsengginseng. The method according to claim 1 , wherein the extract is an ethanol extract extracted from 4˜6 parts by weight of the and has 25˜35% content of ginsenoside claim 1 , the glycyrrhizically related acid is 0.3˜0.5 part by weight of a glycyrrhetic acid having 85˜95% purity claim 1 , and the pharmaceutical composition further comprises a jujuba ethanol extract extracted from 0.08˜0.12 part by weight of a jujuba and having 0.8˜1.2% purity of a jujuba cAMP.7. The method according to claim 1 , wherein the ...

Production of Volatile Dienes by Enzymatic Dehydration of Light Alkenols

Described is a method for generating conjugated dienes through a biological process. More specifically, the application describes a method for producing conjugated dienes (for example butadiene, isoprene or dimethylbutadiene) from light alkenols via enzymatic dehydration, in particular by making use of an alkenol dehydratase.

METHODS AND PHARMACEUTICAL COMPOSITIONS FOR THE TREATMENT OF AUTOIMMUNE DISEASES

The present invention relates to methods and pharmaceutical compositions for the treatment of autoimmune diseases, especially rheumatoid arthritis. More particularly, the present invention relates to an a-enolase polypeptide for use in the prophylactic treatment of an autoimmune disease in a subject in need thereof. 1. A method for the prophylactic treatment of an autoimmune disease in a subject in need thereof comprising administering to the subject a non citrullinated α-enolase polypeptide.2. The method according to wherein the non citrullinated α-enolase polypeptide comprises an amino acid sequence selected from the group consisting of the amino acid sequence ranging from position 5 to position 21 in SEQ ID NO:1 claim 1 , the amino acid sequence ranging from position 6 to position 21 in SEQ ID NO:2 or the amino acid sequence ranging from position 5 to position 21 in SEQ ID NO:3.3. The method according to wherein the non citrullinated α-enolase polypeptide comprises an amino acid sequence selected from the group consisting of CKIHAREIFDSRGNPTVEC (SEQ ID NO:4) claim 1 , CIHAREIFDSRGNPTVEC (SEQ ID NO:5) or CKIIGREILDSRGNPTVEC (SEQ ID NO:6) that is cyclised by a disulfide bound between the two cysteine residues.4. The method according to wherein the non citrullinated α-enolase polypeptide consists of the amino acid sequence SEQ ID NO:1 or the amino acid SEQ ID NO:2 or a functional conservative variant thereof.5. The method according to claim 1 , wherein said autoimmune disease is rheumatoid arthritis. The present invention relates to methods and pharmaceutical compositions for the treatment of autoimmune diseases, especially rheumatoid arthritis.Rheumatoid arthritis (RA), whose prevalence is around 1% in the world, is a chronic inflammatory disorder characterized by synovial hyperplasia leading to joint destruction. This disease affects more often 35-50 years-old women with a sex-ratio=4/1 and is responsible of major disability. In this regard, it represents a public ...

METHODS OF PRODUCING PROTOPORPHYRIN IX AND BACTERIAL MUTANTS THEREFOR

The presently disclosed inventive concepts are directed in certain embodiments to a method of producing protoporphyrin IX by (1) cultivating a strain of bacteria in a culture medium under conditions suitable for growth thereof, and (2) recovering the protoporphyrin IX from the culture medium. The strain of bacteria comprises at least one mutant hemH gene which is incapable of normal expression, thereby causing an accumulation of protoporphyrin IX. In certain embodiments of the method, the strain of bacteria is a strain of , and more specifically may be PV-4. In certain embodiments, the mutant hemH gene of the strain of bacteria may be a mutant of shew_2229 and/or of shew_1140. In other embodiments, the presently disclosed inventive concepts are directed to mutant strains of bacteria having at least one mutant hemH gene which is incapable of normal expression, thereby causing an accumulation of protoporphyrin IX during cultivation of the bacteria. In certain embodiments the strain of bacteria is a strain of , and more specifically may be PV-4. In certain embodiments, the mutant hemH gene of the strain of bacteria may be a mutant of shew_2229 and/or shew_1140. 1. A method of producing protoporphyrin IX , comprising:{'i': Shewanella', 'Shewanella, 'cultivating a strain of bacteria in a culture medium under conditions suitable for growth thereof, the strain of bacteria comprising at least one mutant hemH gene which is incapable of normal expression, thereby causing an accumulation of protoporphyrin IX; and'}recovering the protoporphyrin IX from the culture medium.2ShewanellaS. loihica.. The method of claim 1 , wherein the strain of bacteria is a strain of3ShewanellaS. loihica. The method of claim 1 , wherein the strain of bacteria is PV-4.4. The method of claim 1 , wherein the mutant hemH gene is a mutant of shew2229 and/or a mutant of shew1140.5. The method of claim 1 , wherein the protoporphyrin IX produced in the culture medium is recoverable in an amount of at least ...

ULTRA-PURE AGONISTS OF GUANYLATE CYCLASE C, METHOD OF MAKING AND USING SAME

The invention provides processes of purifying a peptide including a GCC agonist sequence selected from the group consisting of SEQ ID NOs: 1-251 described herein. The processes include a solvent exchange step before a freeze-drying (lyophilization) step. 1. A purified peptide comprising the GCC agonist sequence selected from the group consisting of SEQ ID NO: 9 , wherein the purified peptide has the following characteristics:a) has a bulk density of not greater than 0.1 g/mL;b) contains less than 50 ppm acetamide; andd) less than 0.3% alpha-Asp-9-plenacanatide (RRT 1.33).2. The purified peptide of claim 1 , wherein the peptide is stable at 25° C. for at least three months.4. The purified peptide of claim 1 , wherein the peptide has a bulk density of not greater than 0.06 g/mL claim 1 , not greater than 0.05 g/mL claim 1 , or not greater than 0.04 g/mL.5. The purified peptide of claim 1 , wherein the peptide has a chromatographic purity of no less than 95% claim 1 , no less than 96% claim 1 , or no less than 97%.6. The purified peptide of claim 1 , wherein the peptide is substantially free of water.7. The purified peptide of claim 6 , wherein the the water is not greater than 10% claim 6 , not greater than 9% claim 6 , not greater than 8% claim 6 , not greater than 7% claim 6 , not greater than 6% or not greater than 5%.8. The purified peptide of claim 1 , wherein the peptide is further substantially free of one or more impurities selected from acetonitrile claim 1 , alcohols claim 1 , ammonium claim 1 , acetate claim 1 , and TFA.9. The purified peptide of claim 8 , wherein the peptide contains less than 300 ppm acetonitrile.10. The purified peptide of claim 8 , wherein the peptide contains less than 0.1% TFA.11. The purified peptide of claim 8 , wherein the peptide contains less than 1000 ppm isopropanol.12. The purified peptide of claim 8 , wherein the peptide contains less than 600 ppm isopropanol.13. The purified peptide of claim 8 , wherein the peptide contains ...

ENZYMES AND METHODS FOR STYRENE SYNTHESIS

The subject technology generally relates to biosynthesis of styrene. Certain embodiments of the subject technology is based, in part, on the recognition that phenylalanine can be converted to styrene by a two-step pathway of deamination and de-carboxylation, with trans-cinnamic acid (tCA) as the intermediate. Two types of enzymes are directly involved in this process, phenylalanine ammonia lyase (PAL), which converts phenylalanine to tCA, and cinnamic acid decarboxylase, which coverts tCA to styrene. Host cells expressing these two types of enzymes can be cultured in bioreactor to produce styrene from renewable substrates such as glucose. 18-. (canceled)9. A nucleic acid encoding a fusion protein comprising: (a) a first domain comprising a phenylalanine ammonia lyase , and (b) a second domain comprising a cinnamic acid decarboxylase.10. A vector comprising the nucleic acid of .11. A host cell comprising the vector of .1215-. (canceled)16. An isolated nucleic acid encoding a cinnamic acid decarboxylase comprising a mutation at an amino acid residue position corresponding to a position selected from the group consisting of: 155 claim 10 , 156 claim 10 , 159 claim 10 , 162 claim 10 , 163 claim 10 , 164 claim 10 , 172 claim 10 , 173 claim 10 , 174 claim 10 , 175 claim 10 , 187 claim 10 , 188 claim 10 , 189 claim 10 , 190 claim 10 , 191 claim 10 , 192 claim 10 , 193 claim 10 , 194 claim 10 , 195 claim 10 , 196 claim 10 , 226 claim 10 , 227 claim 10 , 280 claim 10 , 285 claim 10 , 286 claim 10 , 287 claim 10 , 291 claim 10 , 326 claim 10 , 331 claim 10 , 360 claim 10 , 361 claim 10 , 395 claim 10 , 396 claim 10 , 398 claim 10 , 440 claim 10 , 441 of SEQ ID NO:8 claim 10 , and combinations thereof.17. A vector comprising the isolated nucleic acid of .18. A host cell comprising the vector of .19. (canceled)20. A host cell comprising: (a) a recombinantly expressed phenylalanine ammonia lyase; (b) a recombinantly expressed cinnamic acid decarboxylase; and (c) a recombinantly ...

CRYSTALLIZED OXALATE DECARBOXYLASE AND METHODS OF USE

Oxalate decarboxylase crystals, including stabilized crystals, such as cross-linked crystals of oxalate decarboxylase, are disclosed. Methods to treat a disorder associated with elevated oxalate concentration using oxalate decarboxylase crystals are also disclosed. Additionally disclosed are methods of producing protein crystals. 18-. (canceled)9. A method of reducing oxalate in a mammal , the method comprising contacting a body fluid of the mammal with a composition comprising oxalate decarboxylase crystals in an extracorporeal device , wherein the amount of the oxalate decarboxylase crystals contained in the extracorporeal device is sufficient to reduce the oxalate.10. The method of claim 9 , wherein the oxalate decarboxylase crystals are covalently linked by a cross-linking agent.11. The method of claim 9 , wherein said crystals are active and stable in the gastrointestinal tract of the mammal.12. The method of claim 9 , wherein said crystals are active and stable at about pH 2 to about pH 8.1314-. (canceled)15. The method of claim 9 , wherein the method results in a reduction of oxalate of at least about 10%.1617-. (canceled)18. A method of treating a disorder associated with elevated oxalate concentration in a mammal claim 9 , the method comprising contacting a body fluid of the mammal with oxalate decarboxylase crystals in an extracorporeal device claim 9 , wherein the amount of the oxalate decarboxylase crystals contained in the extracorporeal device is sufficient to reduce one or more symptoms associated with the disorder.19. The method of claim 18 , wherein the disorder is related to a kidney or a liver function.20. The method of claim 18 , wherein the disorder is selected from the group consisting of primary hyperoxaluria claim 18 , enteric hyperoxaluria claim 18 , idiopathic hyperoxaluria claim 18 , and ethylene glycol poisoning.2133-. (canceled)34. The method of claim 9 , wherein the oxalate decarboxylase crystals are uncrosslinked.35. The method of ...

Recombinant Oxalate Decarboxylase Expressed in Filamentous Fungi

The present invention relates to a recombinant OxDC expressed in a filamentous fungal host cell, methods for constructing a recombinant filamentous fungal host cell, methods for producing recombinant OxDC and the application thereof. The recombinant filamentous fungal host cell comprises one or more copies of OxDC expression cassette integrated in its genome; the expression cassette comprises a promoter, a signal peptide coding sequence, an OxDC coding sequence and a transcription terminator. The host cell can be constructed by random integration or site-specific integration. In addition, the present invention also optimizes the medium formulation for different recombinant filamentous fungal host cells. In the production of the recombinant OxDC, the final yield and enzyme activity were greatly improved. The invention effectively solves the problem that the production of OxDC in the prior art cannot be industrialized on a large scale. 1. A recombinant OxDC , wherein the recombinant OxDC is recombinantly expressed in an infilamentous fungal host cell , resulting in a form and degree of glycosylation different from an original OxDC expressed in an original host cell , wherein the form and degree of glycosylation of the recombinant OxDC is specific to the filamentous fungal host cell.2. The recombinant OxDC according to claim 1 , wherein the recombinant OxDC maintains all or part of an enzyme activity at pH 1.5-7.0; wherein at pH 1.5-2.5 claim 1 , the enzyme activity of the recombinant OxDC was not lower than 10% of the enzyme activity of the recombinant OxDC at an optimum pH claim 1 , not lower than 50% of the enzyme activity of the recombinant OxDC at pH 2.5-4.5 claim 1 , not lower than 25% of the enzyme activity of the recombinant OxD at the pH 4.5-7.0.3. The recombinant OxDC according to claim 1 , wherein the optimum pH of the recombinant OxDC is 2.5-3.5.4Agrocybe aegerita, Agrocybe Cylindracea, Flammulina velutipes, Coriolus versicolor, Postia placenta, Aspergillus ...

TRANSFORMED YEAST PRODUCING NOVEL 1-OCTEN-3-OL, AND PREPARATION METHOD THEREFOR

The present application relates to a method for preparing transformed yeast producing 1-octen-3-ol, and yeast prepared by the method, and is useful in the cosmetic industry and the food development industry which use a scent. 1. A transformed yeast for producing 1-octen-3-ol transformed with a recombinant vector comprising any one base sequence selected from Sequence Listings 9 , 10 , and 11 encoding lipoxygenase and a base sequence of Sequence Listing 12 encoding hydroperoxide lyase.2. A method for producing a transformed yeast for producing 1-octen-3-ol comprising the steps of:isolating total RNA of pine mushroom and synthesizing cDNA;PCR-amplifying a lipoxygenase gene and a hydroperoxide lyase gene from the synthesized cDNA;gene-cloning each of the amplified lipoxygenase gene and hydroperoxide lyase gene in a vector;gene-cloning each of the cloned lipoxygenase gene and hydroperoxide lyase gene in each yeast expression vector; andtransforming and incubating the yeast expression vector into a yeast to confirm the biosynthesis of 1-octen-3-ol.3. The method of claim 2 , wherein the yeast expression vector is a vector selected from a pYES3/CT vector and a pYES2/CT vector.4. The method of claim 3 , wherein the pYES3/CT vector and the pYES2/CT vector are used in a ratio of 1:1.5. The method of claim 2 , wherein the yeast is incubated in a SC medium using 0.01 to 100 mM of linoleic acid at 15° C. to 45° C. for 12 to 48 hours.6S. cerevisiae. The method of claim 2 , wherein the yeast is Saccharomyces cerevisiae ().7. A method for producing 1-octen-3-ol comprising the steps of:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, 'biosynthesizing 1-octen-3-ol by incubating the transformed yeast for producing the 1-octen-3-ol of in a medium; and'}obtaining the biosynthesized 1-octen-3-ol. This application includes an electronically submitted sequence listing in .txt format. The .txt file contains a sequence listing entitled “3884-0208PUS1_ST25.txt” created on Sep. 1, 2020 and is ...

METHODS, SYNTHETIC HOSTS AND REAGENTS FOR THE BIOSYNTHESIS OF HYDROCARBONS

Systems, networks, methods, compositions and recombinant hosts for biosynthesizing hydrocarbons from a feedstock, such as gas, are provided. 1: A method for biosynthesising a hydrocarbon in a recombinant host , said method comprising:providing a fermentation reactor, the fermentation reactor comprising at least one recombinant host, wherein said recombinant host comprises an exogenous nucleic acid sequence encoding a polypeptide having an enzyme activity of EC 2.2.1.7, andproviding a stream comprising a gas or a biological or nonbiological feedstock to the fermentation reactor, andoperating the fermentation reactor at conditions for said recombinant host to metabolize the gas or feedstock and produce the hydrocarbon.3: The method according to claim 1 , wherein said polypeptide having an enzyme activity of EC 2.2.1.7 converts glyceraldehyde-3-phosphate and pyruvate to 1 deoxy-d-xylulose-phosphate.4: The method according to claim 1 , wherein said polypeptide having an enzyme activity of EC 2.2.1.7 is:(i) encoded by a nucleic acid sequence having at least 49% sequence identity to the nucleic acid sequence set forth in SEQ ID NO:4 or 5 or a functional fragment thereof;(ii) encoded by a nucleic acid sequence comprising the nucleic acid sequence set forth in SEQ ID NO:4 or 5 or a functional fragment thereof;(iii) has at least 49% sequence identity to the amino acid sequence set forth in SEQ ID NO:1 or 2 or a functional fragment thereof; or(iv) comprises the amino acid sequence set forth in SEQ ID NO: 1 or 2 or a functional fragment thereof.57-. (canceled)8: The method according to claim 1 , wherein the recombinant host further comprises an exogenous nucleic acid sequence encoding a polypeptide having an enzyme activity of EC 4.2.3.27.10: The method according to claim 8 , wherein said polypeptide having an enzyme activity of EC 4.2.3.27 is:(i) encoded by a nucleic acid sequence having at least 70% sequence identity to the nucleic acid sequence set forth in SEQ ID NO: 6 or ...

Transgenic microorganisms and synthesis of piperazic acid, piperazic acid containing products, and derivatives thereof

Among the various aspects of the present disclosure is the provision of a biological and biochemical production of piperazic acid derived from the newly discovered production pathway for L-piperazic acid. One aspect of the present disclosure includes a transgenic microorganism (e.g., bacteria) engineered to accumulate piperazic acid and derivatives thereof, including a piperazic acid (Piz)-containing product. Another aspect of the present disclosure includes biochemical and biological methods for producing piperazic acid and derivatives thereof, including a piperazic acid (Piz)-containing product. Another aspect of the present disclosure includes compositions and methods of using isotopically labeled piperazic acid and derivatives thereof, including a piperazic acid (Piz)-containing product.

METHODS AND COMPOSITIONS FOR THE TREATMENT AND/OR PREVENTION OF TYPE 1 DIABETES

The disclosure relates generally to methods and compositions of treating or preventing diabetes mellitus by administering to a subject a composition comprising an amount of stem and/or progenitor cells and at least one antigen-specific therapy. 1. A composition comprising an amount of purified allogenic endothelial progenitor cells and an amount of at least one immunoglobulin-polypeptide chimera , wherein the immunoglobulin-peptide chimera expresses a disease-specific T- or B-cell epitope.2. The composition of claim 1 , wherein the purified endothelial progenitor cells are isolated from bone marrow.3. The composition of claim 1 , wherein the purified endothelial progenitor cells are purified bone marrow endothelial progenitor cells.4. The composition of claim 1 , wherein the immunoglobulin-polypeptide chimera is soluble.5. The composition of claim 1 , wherein the immunoglobulin-polypeptide chimera is aggregated.6. The composition of claim 1 , wherein the immunoglobulin-polypeptide chimera comprises an immunoglobulin having a CDR3 region claim 1 , and wherein a diabetogenic epitope is inserted within the CDR3 region.7. The composition of claim 6 , wherein the diabetogenic epitope comprises GAD2 (SEQ ID NO: 1) claim 6 , GAD1 (SEQ ID NO: 2) or INSβ (SEQ ID NO: 3).8. The composition of comprising no other cell types other than the purified endothelial progenitor cells.9. The composition of claim 1 , wherein the composition comprises no or substantially no cells that are Lin claim 1 , c-Kit claim 1 , and/or FLK-1.10. A composition comprising:an amount of cells, wherein the cells consist essentially of purified allogenic endothelial progenitor cells; andan amount of at least one immunoglobulin-polypeptide chimera, wherein the immunoglobulin-peptide chimera expresses a disease-specific T- or B-cell epitope.11. The composition of claim 10 , wherein the immunoglobulin-polypeptide chimera comprises an immunoglobulin having a CDR3 region claim 10 , and wherein a diabetogenic ...

REPAIR OF UV-INDUCED DNA LESIONS

A composition comprising a recombinant enzyme that comprises a fusion of: a cyclobutane pyrimidine dimer photolyase corresponding to an amino acid encoding sequence having at least 85% sequence identity to SEQ ID NO 1, a pyrimidine(6-4)pyrimidone photolyase corresponding to an amino acid encoding sequence having at least 85% sequence identity to SEQ ID NO 2, and a skin penetrating peptide. 115.-. (canceled)16. A composition comprising a recombinant enzyme that comprises a fusion of a cyclobutane pyrimidine dimer photolyase , a pyrimidine(6-4)pyrimidone photolyase and a skin penetrating peptide ,wherein said cyclobutane pyrimidine dimer photolyase corresponds to an amino acid encoding sequence having at least 85% sequence identity to SEQ ID NO 1,wherein said pyrimidine(6-4)pyrimidone photolyase corresponds to an amino acid encoding sequence having at least 85% sequence identity to SEQ ID NO 2.17. The composition of claim 16 , wherein said skin penetrating peptide is encoded by the DNA sequence SEQ ID NO 3.18. The composition of claim 16 , wherein said recombinant enzyme is a deazaflavin photolyase.19. The composition of claim 16 , wherein said recombinant enzyme comprises one or more tag peptides to facilitate purification of the recombinant enzyme.20. The composition of claim 16 , further comprising a carrier and/or an excipient to facilitate uptake of the composition in or on the body.21. The composition of claim 20 , wherein said carrier and/or said excipient comprises an encapsulating material for at least temporarily encapsulating at least said cyclobutane pyrimidine dimer photolyase and said pyrimidine(6-4)pyrimidone photolyase.22. The composition of claim 21 , wherein said carrier and/or said excipient comprises a liposome and/or thermoresponsive polyglycerol particles.23. The composition of claim 16 , further comprising a solubilizer claim 16 , a skin permeation enhancer claim 16 , a preservative claim 16 , a moisturizer claim 16 , a gelling agent claim 16 , ...

USE OF GENETICALLY ENGINEERED STRAIN VNP20009-M IN PREVENTING AND TREATING CANCER METASTASIS

The present disclosure provides uses of genetically engineered attenuated strain VNP20009-M in preventing and treating cancer metastasis. The genetically engineered strain VNP20009-M is targeted to cancer cells and has a significant effect of inhibiting metastasis and growth. VNP20009-M can be used to prepare medicaments for the prevention and treatment of tumor metastasis. 1Salmonella typhimurium. A method for preventing or treating metastasis of a cancer in a subject , the method comprising administering a therapeutically effective amount of a genetically engineered strain VNP20009-M to the subject , wherein the genetically engineered strain VNP20009-M is an attenuated VNP20009 comprising an L-methioninase gene.2Salmonella typhimurium. The method according to claim 1 , wherein the genetically engineered bacterium VNP20009-M is an attenuated VNP20009 which comprises a vector comprising the L-methioninase gene.3. The method according to claim 1 , wherein the cancer is selected from the group consisting of lung cancer claim 1 , breast cancer claim 1 , prostate cancer claim 1 , pancreatic cancer claim 1 , liver cancer claim 1 , colon cancer claim 1 , rectal cancer claim 1 , gastric cancer claim 1 , esophageal cancer claim 1 , laryngeal cancer claim 1 , leukemia claim 1 , lymphoma claim 1 , melanoma claim 1 , uterine cancer claim 1 , ovarian cancer claim 1 , skin cancer claim 1 , bronchial carcinoma claim 1 , bronchiolar carcinoma claim 1 , urethral cancer claim 1 , kidney cancer claim 1 , oral cancer claim 1 , vaginal cancer claim 1 , cholangiocarcinoma claim 1 , bladder cancer and nasopharyngeal carcinoma.4Salmonella typhimurium. The method according to claim 2 , wherein the genetically engineered strain VNP20009-M is constructed according to the following method: inserting the L-methioninase gene into the plasmid to obtain an L-methioninase expression plasmid; electro-transforming the L-methioninase expression plasmid to attenuated VNP20009; and obtaining the ...

PHARMACEUTICAL COMPOSITION COMPRISING ERYTHROCYTES ENCAPSULATING A PLP-DEPENDENT ENZYME AND, A NON-PHOSPHATE PLP PRECURSOR

The invention relates to a pharmaceutical composition containing a PLP-dependent enzyme and optionally its cofactor, pyridoxal phosphate (PLP), and/or a phosphate or non-phosphate precursor of PLP, its use as a drug, its production method and a therapeutic treatment method related to it. The pharmaceutical composition comprises erythrocytes and a pharmaceutically acceptable vehicle, the erythrocytes encapsulating the PLP-dependent enzyme. The PLP-dependent enzyme may be methioninase, tyrosine phenol-lyase, tyrosine aminotransferase or cystathionine beta-synthase. 125-. (canceled)26. . One or more erythrocyte(s) encapsulating a plurality of PLP-dependent enzyme molecules , the erythrocytes comprising a sufficient amount of PN-kinase and PNP oxidase to produce a sufficient amount of PLP from PLP precursor present in a patient or subject's bloodstream to maintain a sufficient portion of the erythrocyte-encapsulated PLP-dependent enzyme molecules in their holoenzyme forms to preserve enzymatic activity beyond 24 hours after injection or infusion into the patient or subject in need of said enzymatic activity.27. The erythrocyte(s) of claim 26 , wherein the PLP-dependent activity persists in the patient or subject for at least 1 claim 26 , 5 claim 26 , 10 or 15 days after injection or infusion.28. The erythrocyte(s) of claim 26 , wherein the PLP-dependent activity persists in the patient or subject for at least 15 days after injection or infusion as measured by a depletion of more than 20 claim 26 , 30 claim 26 , 40 or 50% of the PLP-dependent enzyme's substrate in the plasma of the patient or subject.29. A method of using the erythrocyte(s) of claim 26 , in any one or more of the following methods:(a) a therapeutic treatment method for a patient or subject in need of long lasting PLP-dependent enzymatic activity;(b) a therapeutic treatment method for depleting or reducing a plasma or circulating substrate selected from methionine, homocysteine and tyrosine in a patient ...

COMPOSITIONS AND METHODS OF USING CHONDROITINASE ABCI MUTANTS

One aspect of the present invention relates to mutants of chondroitinase ABCI. Such chondroitinase ABCI mutants exhibit altered chondroitin lyase activity or increased resistance to inactivation from stressors including exposure to UV light or heat. Methods of using chondroitinase ABCI mutant enzymes are also provided. 1. An isolated nucleic acid comprising a cDNA sequence that encodes for a mutant chondroitinase ABC I polypeptide selected from the group consisting of SEQ ID NO: 1 , SEQ ID NO: 2 , SEQ ID NO: 3 , SEQ ID NO: 4 , SEQ ID NO: 5 , SEQ ID NO: 6 , and SEQ ID NO: 7.2. The nucleic acid of claim 1 , wherein the cDNA sequence encodes for the mutant chondroitinase ABC I polypeptide of SEQ ID NO:1.3. The nucleic acid of claim 1 , wherein the cDNA sequence encodes for the mutant chondroitinase ABC I polypeptide of SEQ ID NO:2.4. The nucleic acid of claim 1 , wherein the cDNA sequence encodes for the mutant chondroitinase ABC I polypeptide of SEQ ID NO:3.5. The nucleic acid of claim 1 , wherein the cDNA sequence encodes for the mutant chondroitinase ABC I polypeptide of SEQ ID NO:4.6. The nucleic acid of claim 1 , wherein the cDNA sequence encodes for the mutant chondroitinase ABC I polypeptide of SEQ ID NO:5.7. The nucleic acid of claim 1 , wherein the cDNA sequence encodes for the mutant chondroitinase ABC I polypeptide of SEQ ID NO:6.8. The nucleic acid of claim 1 , wherein the cDNA sequence encodes for the mutant chondroitinase ABC I polypeptide of SEQ ID NO:7.9. A composition comprising an isolated nucleic acid sequence that encodes for a mutant chondroitinase ABC I polypeptide selected from the group consisting of SEQ ID NO: 1 claim 1 , SEQ ID NO: 2 claim 1 , SEQ ID NO: 3 claim 1 , SEQ ID NO: 4 claim 1 , SEQ ID NO: 5 claim 1 , SEQ ID NO: 6 claim 1 , and SEQ ID NO: 7.10. The composition of claim 9 , wherein the isolated nucleic acid sequence is present in effective amount. This application is a continuation application of U.S. application Ser. No. 14/480,486, ...

METHODS AND HOST CELLS FOR ENHANCING PRODUCTION OF 1, 3-BUTANEDIOL

This application describes non-naturally occurring host cells for enhanced 1,3-butanediol (1,3-BDO) production, methods for producing 1,3-BDO using such non-naturally occurring host cells, and 1,3-BDO products produced by such non-naturally occurring host cells and methods. 1. A non-naturally occurring host cell capable of enhanced 1 ,3-butanediol production , comprising: (i) decrease or inhibit the activity of a polypeptide having the activity of an enzyme of EC 4.1.1.5, or', '(ii) decrease or prevent expression of a gene encoding a polypeptide having the activity of an enzyme of EC 4.1.1.5, and, '(a) a modification to either (i) decrease or inhibit the activity of a polypeptide having the activity of an enzyme of EC 1.2.1.10, or', '(ii) decrease or prevent expression of a gene encoding a polypeptide having the activity of an enzyme of EC 1.2.1.10,, '(b) a modification to eitherwherein, compared to an unmodified host cell, the non-naturally occurring host cell:(i) gains three reducing equivalents,(ii) gains three chemical species, wherein said chemical species are capable of transferring the equivalent of one electron in a redox reaction, or(iii) produces more 1,3-butanediol.2. The non-naturally occurring host cell of claim 1 , wherein the modifications comprise at least one gene knockout.3. The non-naturally occurring host cell of claim 1 , wherein the host comprises one or more exogenous nucleic acids encoding one or more polypeptides having the activity of one or more enzymes chosen from:(a) an enzyme of EC 2.3.1.9;(b) an enzyme of EC 1.1.1.36;(c) an enzyme of EC 1.1.1.157;(d) an enzyme of EC 2.8.3.-;(e) an enzyme of EC 1.2.99.6; and(g) an enzyme of EC 1.1.1.-.4. The non-naturally occurring host cell of claim 1 , wherein the host expresses one or more polypeptides having the activity of one or more enzymes chosen from:(a) an enzyme of EC 2.3.1.8; and(b) an enzyme of EC 2.7.2.15.5. The non-naturally occurring host cell of claim 3 , wherein the enzyme of EC 2.8.3 ...

AADC POLYNUCLEOTIDES FOR THE TREATMENT OF PARKINSON'S DISEASE

The disclosure relates to compositions and methods for the preparation, manufacture and therapeutic use of polynucleotides encoding AADC for the treatment of Parkinson's Disease. 1. An AAV vector genome comprising , in order:a) a 5′ inverted terminal repeat (ITR), wherein said 5′ ITR is 141 nucleotides in length;b) an AADC sequence region, said AADC sequence region comprising a nucleotide sequence encoding SEQ ID NO: 1,c) a 3′ ITR, wherein said 3′ ITR is 141 nucleotides in length.2. The AAV vector genome of claim 1 , wherein the 5′ ITR and the 3′ ITR are derived from AAV2.3. The AAV vector genome of claim 2 , wherein the AAV vector genome comprises a cytomegalovirus (CMV) sequence region derived from a CMV gene; wherein the CMV sequence region comprises an enhancer region and promoter region.4. The AAV vector genome of claim 3 , wherein the CMV sequence region is 507 nucleotides in length.5. The AAV vector genome of claim 2 , wherein the AAV vector genome comprises an immediate early 1 (IE1) sequence region derived from an IE1 gene.6. The AAV vector genome of claim 5 , wherein the IE1 sequence region comprises a nucleotide sequence from IE1 exon1.7. The AAV vector genome of claim 6 , wherein the IE1 sequence region comprises a nucleotide sequence from IE1 intron 1 or a fragment thereof.8. The AAV vector genome of claim 7 , wherein the IE1 sequence region is 166 nucleotides in length.9. The AAV vector genome of claim 2 , wherein the AAV vector genome comprises a human beta globin (BB) sequence region derived from a HB gene.10. The AAV vector genome of claim 9 , wherein the HB sequence region comprises a nucleotide sequence from HB intron 2.11. The AAV vector genome of claim 10 , wherein the HB sequence region comprises a nucleotide sequence from HB exon 3.12. The AAV vector genome of claim 11 , wherein the HB sequence region is 400 nucleotides in length.13. The AAV vector genome of claim 2 , wherein the AAV vector genome comprises a poly(A) signal sequence region ...

Aadc polynucleotides for the treatment of parkinson's disease

The disclosure relates to compositions and methods for the preparation, manufacture and therapeutic use of polynucleotides encoding AADC for the treatment of Parkinson's Disease.

AADC POLYNUCLEOTIDES FOR THE TREATMENT OF PARKINSON'S DISEASE

The disclosure relates to compositions and methods for the preparation, manufacture and therapeutic use of polynucleotides encoding AADC for the treatment of Parkinson's Disease. 1. An AAV vector genome comprising , in order:a) a 5′ inverted terminal repeat (ITR), wherein said 5′ ITR is 119 nucleotides in length;b) an AADC sequence region, said AADC sequence region comprising a nucleotide sequence encoding SEQ ID NO: 1,c) a 3′ ITR, wherein said 3′ ITR is 130 nucleotides in length.2. The AAV vector genome of claim 1 , wherein the 5′ ITR and the 3′ ITR are derived from AAV2.3. The AAV vector genome of claim 2 , wherein the 5′ ITR consists of a nucleotide sequence consisting of nucleotides 3535 to 3417 of SEQ ID NO 6.4. The AAV vector genome of claim 2 , wherein the 5′ ITR consists of a nucleotide sequence which has at least 99% sequence identity with nucleotides 3535 to 3417 of SEQ ID NO 6.5. The AAV vector genome of claim 3 , wherein the 3′ ITR consists of a nucleotide sequence consisting of nucleotides 130 to 1 of SEQ ID NO 6.6. The AAV vector genome of claim 4 , wherein the 3′ ITR consists of a nucleotide sequence which has at least 99% sequence identity with nucleotides 130 to 1 of SEQ ID NO 6.7. The AAV vector genome of claim 6 , wherein the AAV vector genome comprises a cytomegalovirus (CMV) sequence region derived from a CMV gene; wherein the CMV sequence region comprises an enhancer region and promoter region.8. The AAV vector genome of claim 7 , wherein the CMV sequence region comprises a nucleotide sequence which has at least 99% sequence identity with nucleotides 263 to 769 of SEQ ID NO 6.9. The AAV vector genome of claim 7 , wherein the CMV sequence region comprises a nucleotide sequence which has at least 98% sequence identity with nucleotides 263 to 769 of SEQ ID NO 6.10. The AAV vector genome of claim 8 , wherein the CMV enhancer region comprises a nucleotide sequence which has at least 99% sequence identity with nucleotides 263 to 566 of SEQ ID NO 6.11 ...

Antibodies to argininosuccinate synthase and related methods

Provided are antibodies, and antigen-binding fragments thereof, which specifically bind to argininosuccinate synthase, and related compositions, kits, and methods of use thereof, for instance, as companion diagnostics to identify suitable subjects for arginine deprivation or depletion therapies such as ADI-PEG 20 and other arginine deiminase (ADI) polypeptide-based therapies.

COMPOSITION AND METHODS FOR TREATING ISCHEMIC WOUNDS AND INFLAMMATORY CONDITIONS

Methods, compositions, and treatment protocols for treating ischemic wounds and inflammatory conditions in a patient. The treatment protocols comprise or consist of using a modified collagen gel (MCG) to promote healing of ischemic wounds and reduce inflammation at the wound site and in other inflammatory conditions. The modified collagen gel comprises generally a dispersion of collagens in an aqueous matrix comprising water and glycerine, where the amount of Type I collagen is greater than the amount of Type II and Type III collagens in the gel. 1. A method of treating an ischemic wound in a patient , said patient having an ischemic wound site said method comprising:topically applying or injecting, for a therapeutically effective period of time, a therapeutically effective amount of a modified collagen gel composition to said ischemic wound site to yield a treated ischemic wound site,wherein said modified collagen gel promotes healing of said treated ischemic wound site.2. The method of claim 1 , wherein said modified collagen gel comprises modified collagen of long and short polypeptides claim 1 , dispersed in an aqueous matrix comprising water and glycerine.3. The method of claim 2 , wherein said modified collagen is a hydrolyzed bovine collagen.4. The method of claim 2 , wherein said collagen gel comprises an amount of each of Type I claim 2 , Type II claim 2 , and Type III collagen claim 2 , wherein the amount of Type I collagen is greater than the amount of Type II or Type III collagen claim 2 , and wherein the amount of Type III collagen is greater than the amount of Type II collagen.5. The method of claim 2 , wherein said modified collagen gel comprises from about 25 to about 75% by weight modified collagen dispersed in said aqueous matrix claim 2 , based upon the total weight of the gel composition taken as 100% by weight.6. The method of claim 2 , said modified collagen gel further comprising hemoglobin and/or carbonic anhydrase II.7. The method of claim 1 ...

METHODS AND COMPOSITIONS FOR PREPARING TAGATOSE FROM FRUCTOSE

Disclosed herein are compositions and methods for preparing tagatose from fructose, more particularly, compositions comprising thermophilic fructose C4-epimerases derived from thermophilic microorganisms and methods for preparing tagatose from fructose using the compositions. 1294-. (canceled)295. A method of producing tagatose , comprising:contacting fructose with a modified polypeptide comprising one or more modifications as compared to an unmodified polypeptide, the unmodified polypeptide being SEQ ID: 6, whereinthe modified polypeptide converts the fructose to the tagatose through epimerization at the carbon-4 position of the fructose, andthe modified polypeptide comprises at least 85% identity to SEQ ID NO: 6.296. The method of claim 295 , wherein the one or more modifications of the modified polypeptide include one or more amino acid substitutions of lysine residues of SEQ ID NO: 6 claim 295 , the one or more amino acid substitutions of the lysine residues of SEQ ID NO: 6 reducing a total number of exposed lysine residues and reducing claim 295 , when compared to the unmodified polypeptide claim 295 , susceptibility of the modified polypeptide to inactivation.297. The method of claim 296 , wherein the one or more amino acid substitutions of SEQ ID NO: 6 are selected from the group consisting of K67 claim 296 , K78 claim 296 , K137 claim 296 , K221 claim 296 , K229 claim 296 , K321 claim 296 , K384 claim 296 , and K393.298. The method of claim 297 , wherein the K at position 67 is substituted with ARG.299. The method of claim 297 , wherein the K at position 78 is substituted with GLN.300. The method of claim 297 , wherein the K at position I37 is substituted with VAL or THR.301. The method of claim 297 , wherein the K at position 221 is substituted with GLN.302. The method of claim 297 , wherein the K at position 229 is substituted with SER or ASN.303. The method of claim 297 , wherein the K at position 321 is substituted with SER.304. The method of claim 297 , ...

Herbicide-resistant rice plants, polynucleotides encoding herbicide-resistant acetohydroxyacid synthase large subunit proteins, and methods of use

Herbicide-resistant rice plants, isolated polynucleotides that encode herbicide resistant and wild-type acetohydroxy-acid synthase large subunit 1 (AHASL1) polypeptides, and the amino acid sequences of these polypeptides, are described. Expression cassettes and transformation vectors comprising the polynucleotides of the invention, as well as plants and host cells transformed with the polynucleotides, are described. Methods of using the polynucleotides to enhance the resistance of plants to imidazolinone herbicides, and methods for controlling weeds in the vicinity of herbicide-resistant plants are also described.

ENGINEERED DEOXYRIBOSE-PHOSPHATE ALDOLASES

The present invention provides engineered deoxyribose-phosphate aldolase polypeptides useful under industrial process conditions for the production of pharmaceutical and fine chemical compounds. 1. An engineered deoxyribose-phosphate aldolase comprising a polypeptide sequence having at least 85% , 86% , 87% , 88% , 89% , 90% , 91% , 92% , 93% , 94% , 95% , 96% , 97% , 98% , 99% , or more sequence identity to SEQ ID NOS: 2 , 6 , and/or 466 , or a functional fragment thereof , wherein said engineered deoxyribose-phosphate aldolase comprises at least one substitution or substitution set in said polypeptide sequence , and wherein the amino acid positions of said polypeptide sequence are numbered with reference to SEQ ID NO: 2 , 6 , and/or 466.2. The engineered deoxyribose-phosphate aldolase of claim 1 , wherein said polypeptide sequence has at least 85% claim 1 , 86% claim 1 , 87% claim 1 , 88% claim 1 , 89% claim 1 , 90% claim 1 , 91% claim 1 , 92% claim 1 , 93% claim 1 , 94% claim 1 , 95% claim 1 , 96% claim 1 , 97% claim 1 , 98% claim 1 , 99% claim 1 , or more sequence identity to SEQ ID NO:2 claim 1 , wherein said engineered deoxyribose-phosphate aldolase comprises at least one substitution or substitution set in said polypeptide sequence at one or more positions selected from 10/47/66/141/145/156 claim 1 , 2 claim 1 , 6 claim 1 , 9 claim 1 , 10/47/88/156 claim 1 , 13 claim 1 , 31 claim 1 , 46 claim 1 , 47 claim 1 , 47/134/141/212 claim 1 , 66 claim 1 , 66/88/112/134/141/143/145/212 claim 1 , 71 claim 1 , 72 claim 1 , 88 claim 1 , 94 claim 1 , 102 claim 1 , 104 claim 1 , 112 claim 1 , 116 claim 1 , 133 claim 1 , 133/173/204/235/236 claim 1 , 134 claim 1 , 145 claim 1 , 145/173 claim 1 , 147 claim 1 , 173 claim 1 , 184 claim 1 , 189 claim 1 , 197 claim 1 , 203 claim 1 , 204 claim 1 , 207 claim 1 , 226 claim 1 , 235 claim 1 , 235/236 claim 1 , and 236 claim 1 , and wherein the amino acid positions of said polypeptide sequence are numbered with reference to SEQ ID NO: ...

NEAR-INFRARED LIGHT-ACTIVATED PROTEINS

Methods and constructs are provided for controlling processes in live animals, plants or microbes via genetically engineered near-infrared light-activated or light-inactivated proteins including chimeras including the photosensory modules of bacteriohytochromes and output modules that possess enzymatic activity and/or ability to bind to DNA, RNA, protein, or small molecules. DNA encoding these proteins are introduced as genes into live animals, plants or microbes, where their activities can be turned on by near-infrared light, controlled by the intensity of light, and turned off by near-infrared light of a different wavelength than the activating light. These proteins can regulate diverse cellular processes with high spatial and temporal precision, in a nontoxic manner, often using external light sources. For example, near-infrared light-activated proteins possessing nucleotidyl cyclase, protein kinase, protease, DNA-binding and RNA-binding activities are useful to control signal transduction, cell apoptosis, proliferation, adhesion, differentiation and other cell processes. 1. A homodimeric fusion protein controllable by far red and/or near-infrared (NIR) light , said fusion protein comprising a photoreceptor module comprising:a. a bacteriophytochrome; and (1) a photoreceptor module of a bacteriophytochrome; and', '(2) a heterologous output module capable of being activated upon homodimerization to perform said desired activity;', 'wherein said monomers are not active when separated, but are capable of combining to form homodimers that are controllable by far red or NIR light., 'b. a heterologous output module capable of producing a desired activity; wherein said homodimeric fusion protein comprises two monomers that each comprise2. The homodimeric fusion protein of also comprising a linker sequence between said photoreceptor module and said output module.3. The homodimeric fusion protein of made by a method comprising:a. identifying candidate output domains based ...

Bacteria Engineered to Reduce Hyperphenylalaninemia

Genetically engineered bacteria, pharmaceutical compositions thereof, and methods of modulating and treating diseases associated with hyperphenylalaninemia are disclosed. 1. A bacterium comprising:a) one or more gene(s) encoding a phenylalanine ammonia lyase (PAL), wherein the gene(s) encoding a PAL is operably linked to a directly or indirectly inducible promoter that is not associated with the PAL gene in nature; andb) one or more gene(s) encoding a phenylalanine transporter, wherein the gene(s) encoding the phenylalanine transporter is operably linked to a directly or indirectly inducible promoter that is not associated with the phenylalanine transporter gene in nature.2. The bacterium of claim 1 , further comprising one or more gene(s) encoding an L-aminoacid deaminase (LAAD) claim 1 , wherein the gene(s) encoding LAAD is operably linked to a directly or indirectly inducible promoter that is not associated with the LAAD gene in nature.3. The bacterium of claim 2 , wherein the promoter operably linked to the gene(s) encoding a PAL and the promoter operably linked to the gene(s) encoding a phenylalanine transporter are separate copies of the same promoter.4. The bacterium of claim 2 , wherein the gene(s) encoding a LAAD is operably linked to a different promoter from the promoter operably linked to the gene(s) encoding a PAL and the gene(s) encoding a phenylalanine transporter.5. The bacterium of claim 2 , wherein the promoter or promoters operably linked to the gene(s) encoding a PAL and the gene(s) encoding a phenylalanine transporter are directly or indirectly induced by exogenous environmental conditions found in a mammalian gut.6. The bacterium of claim 2 , wherein the promoter or promoters operably linked to the gene(s) encoding a PAL and the gene(s) encoding a phenylalanine transporter are directly or indirectly induced under low-oxygen or anaerobic conditions.7. The bacterium of claim 6 , wherein the promoter or promoters are selected from the group ...

METHODS AND COMPOSITIONS FOR THE TREATMENT AND/OR PREVENTION OF TYPE 1 DIABETES

The disclosure relates generally to methods and compositions of treating or preventing diabetes mellitus by administering to a subject a composition comprising an amount of stem and/or progenitor cells and at least one antigen-specific therapy.

VITAMIN PROTOTROPHY AS A SELECTABLE MARKER

One or more genes in a biosynthesis pathway for a vitamin or other essential nutrient which is needed for the survival of a microorganism can be used as an effective selective marker to identify cells transformed with an exogenous nucleic acid. The microorganism does not naturally contain or express the one or more gene. This permits genetic manipulations to be performed. It permits lower cost fermentations to be performed. It permits production of the essential nutrient for subsequent commodity use. 1. A method of using vitamin prototrophy as a selectable marker comprising:(a) transforming a microorganism auxotrophic for a vitamin with both a vitamin biosynthesis gene and a gene conferring a desired property, wherein the microorganism is not transformed with an antibiotic resistance gene and(b) culturing the microorganism in the absence of the vitamin,wherein growth of the microorganism in the absence of the vitamin indicates successful transformation of the microorganism with both the vitamin biosynthesis gene and the gene conferring a desired property.2. The method of claim 1 , wherein the culturing is performed in the absence of an antibiotic.3. The method of claim 1 , wherein antibiotic resistance is not used as a selectable marker.4. The method of claim 1 , wherein transformation with the vitamin biosynthesis gene renders the microorganism prototrophic for the vitamin.5. The method of claim 1 , wherein the desired property is not selectable.6. The method of claim 1 , wherein the vitamin is thiamine.7. The method of claim 1 , wherein the vitamin biosynthesis gene encodes thiamine biosynthesis protein (ThiC) (EC 4.1.99.17).8Clostridium ragsdalei.. The method of claim 1 , wherein the vitamin biosynthesis gene is thiC derived from9. The method of claim 1 , wherein the vitamin is pantothenate.10. The method of claim 1 , wherein the vitamin biosynthesis gene encodes methyl-2-oxobutanoate hydroxymethyltransferase (PanB) (EC 2.1.2.11) claim 1 , pantoate-beta-alanine ...

METHOD FOR PRODUCING 1,3-PROPANEDIOL USING MICROORGANISM VARIANT WITH DELETION OF 2,3-BUTANEDIOL SYNTHETIC GENE

The present invention relates to a method for producing 1,3-propanediol using a mutant microorganism lacking a 2,3-butanediol synthetic gene, and more particularly to a mutant microorganism wherein a gene encoding lactate dehydrogenase and a gene encoding an enzyme which is involved in 2,3-butanediol synthesis are deleted in a microorganism having the ability to produce 1,3-propanediol from glycerol and wherein a gene encoding pyruvate decarboxylase and a gene encoding aldehyde dehydrogenase are introduced or amplified, and to a method of promoting the production of 1,3-propanediol while inhibiting the production of 2,3-butanediol by using the mutant microorganism. The use of the glycerol-fermenting mutant microorganism according to the present invention can significantly increase the production of 1,3-propanediol while minimizing the production of 2,3-butanediol. 1. A mutant microorganism wherein a gene encoding lactate dehydrogenase and a gene encoding an enzyme which is involved in 2 ,3-butanediol synthesis are deleted in a microorganism having the ability to produce 1 ,3-propanediol from glycerol and wherein a gene encoding pyruvate decarboxylase and a gene encoding aldehyde dehydrogenase are introduced or amplified.2. The mutant microorganism of claim 1 , wherein the enzyme which is involved in 2 claim 1 ,3-butanediol synthesis is an acetolactate synthase.3. The mutant microorganism of claim 1 , wherein the gene encoding pyruvate decarboxylase is pdc derived from a stain claim 1 , which has pyruvate decarboxylase activity.4. The mutant microorganism of claim 1 , wherein the gene encoding aldehyde dehydrogenase is aldB derived from a strain claim 1 , which has pyruvate decarboxylase activity.5. The mutant microorganism of claim 1 , which is Klebsiella pneumonia.6. A method for producing 1 claim 1 ,3-propanediol claim 1 , comprising the steps of:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, '(a) culturing the mutant microorganism of in a glycerol-containing ...

USE OF N-ACETYLNEURAMINIC ACID ALDOLASE IN CATALYTIC SYNTHESIS OF N-ACETYLNEURAMINIC ACID

It discloses a use of N-acetylneuraminic acid aldolase with an amino acid sequence as shown in SEQ ID NO: 2 in catalytic synthesis of N-acetylneuraminic acid. The preparation of N-acetylneuraminic acid is to use the N-acetylneuraminic acid aldolase with the amino acid sequence as shown in SEQ ID NO: 2 as a catalyst, and N-acetylmannosamine and pyruvic acid as substrates.

Human Cystathionine Beta-Synthase Variants and Methods of Production Thereof

Human cystathionine β-synthase variants are disclosed, as well as a method to produce recombinant human cystathionine β-synthase and variants thereof. More particularly, the role of both the N-terminal and C-terminal regions of human CBS has been studied, and a variety of truncation mutants and modified CBS homologues are described. In addition, a method to express and purify recombinant human cystathionine β-synthase (CBS) and variants thereof which have only one or two additional amino acid residues at the N-terminus are described.

PLANTS HAVING ENHANCED YIELD-RELATED TRAITS AND A METHOD FOR MAKING THE SAME

The present invention relates to a method for enhancing various yield-related traits by modulating expression in a plant of a nucleic acid encoding an Ornithine Decarboxylase (ODC) polypeptide, a benzothiadiazole-induced homeodomain 1 (BIHD1) polypeptide, a MYB30, a THOM (tomato homeobox) protein, or a benzothiadiazole-induced homeodomain 2 (BIHD2) polypeptide. The present invention also concerns plants having modulated expression of such a nucleic acid, which plants have enhanced yield-related traits relative to corresponding control plants. The invention also provides constructs useful in the methods of the invention.

ENGINEERED PHENYLALANINE AMMONIA LYASE POLYPEPTIDES

The present invention provides engineered phenylalanine ammonia-lyase (PAL) polypeptides and compositions thereof, as well as polynucleotides encoding the engineered phenylalanine ammonia-lyase (PAL) polypeptides. 1. An engineered polypeptide comprising an amino acid sequence having at least 90% sequence identity to reference sequence SEQ ID NO:4 , wherein said amino acid sequence comprises a glycine at position 290 , and wherein the positions in said amino acid sequence are in reference to SEQ ID NO:4.2. The engineered polypeptide of claim 1 , wherein said engineered polypeptide further comprises at least one or more of the following substitutions or substitution sets selected from 39/91/158/180/195/256/290/399/459/463 claim 1 , 39/91/158/180/290/394/399/474/522/524 claim 1 , 39/91/256/290/394/399/404/407/522/524 claim 1 , 91/158/243/256/290/399/407/459/463/474/522/524 claim 1 , and 256/290/404/407/474/522 claim 1 , wherein said positions in said amino acid sequence are in reference to SEQ ID NO:4.3. The engineered polypeptide of claim 1 , wherein said engineered polypeptide further comprises at least one or more of the following substitutions or substitution sets selected from 39/91/256/290/307/399/404/407/522/524 claim 1 , 39/91/256/290/307/404/407/524 claim 1 , 39/91/256/290/399/404/407/522 claim 1 , 39/91/290/307/407 claim 1 , 39/91/290/307/407/524 claim 1 , and 39/256/290/307/404/407 claim 1 , wherein said positions in said amino acid sequence are in reference to SEQ ID NO:4.4. An engineered polypeptide comprising an amino acid sequence having at least 90% sequence identity to reference sequence SEQ ID NO:10 claim 1 , wherein said amino acid sequence comprises a glycine at position 290 claim 1 , and wherein said engineered polypeptide further comprises at least one or more of the following substitutions or substitution sets selected from 32/54/73/305/503/521/565 claim 1 , 32/59/73/240/503/565 claim 1 , 32/59/73/240/565 claim 1 , 54/59/73/305/503/521/565 claim ...

COMPOSITIONS AND METHODS FOR THE TREATMENT OF CNS INJURIES

The present invention is directed to a method of improving functional recovery following a central nervous system contusion injury. The method includes administering a therapeutically effective amount of glycosaminoglycan degrading enzyme. The glycosaminoglycan degrading enzyme may be dermatan sulfate or chondroitin sulfate degrading enzymes. The central nervous system contusion injury may include a traumatic brain injury or a spinal cord injury. The functional recovery may include autonomic functions, sensory functions, motor functions or the like. 116-. (canceled)17. A method of improving autonomic function of the central nervous system comprising administering chondroitinase ABCenzyme to a mammal following a contusion injury caused by bruised or crushed neurons in the central nervous system and not severed neurons , wherein the autonomic function is improved.18. The method of claim 17 , wherein the chondroitinase ABCenzyme administered to the mammal comprises a therapeutically effective amount.19. The method of claim 18 , wherein the therapeutically effective amount of chondroitinase ABCenzyme comprises an amount sufficient to degrade chondroitin sulfate proteoglycans.20. The method of claim 19 , wherein the degradation of the chondroitin sulfate proteoglycans occurs at the site of the central nervous system injury.21. The method of claim 18 , wherein the therapeutically effective amount of chondroitinase ABCenzyme comprises a maximum of about 100 mg/kg.22. The method of claim 17 , wherein the chondroitinase ABCenzyme is administered locally.23. The method of claim 22 , wherein the local administration is selected from the group consisting of intrathecal and topical administration.24. The method of claim 17 , wherein the chondroitinase ABCenzyme is in a sustained release formulation.25. The method of claim 19 , wherein the degradation of the chondroitin sulfate proteoglycans occurs outside the site of the contusion injury.26. The method of claim 17 , wherein the ...

ENGINEERED PHENYLALANINE AMMONIA LYASE POLYPEPTIDES

The present invention provides engineered phenylalanine ammonia lyase (PAL) polypeptides and compositions thereof, as well as polynucleotides encoding the engineered phenylalanine ammonia lyase (PAL) polypeptides. Methods for producing PAL enzymes are also provided. In some embodiments, the engineered PAL polypeptides are optimized to provide enhanced catalytic activities that are useful under industrial process conditions for the production of pharmaceutical compounds. 1. An engineered phenylalanine ammonia lyase comprising a polypeptide sequence having at least 85% , 86% , 87% , 88% , 89% , 90% , 91% , 92% , 93% , 94% , 95% , 96% , 97% , 98% , 99% , or more sequence identity to SEQ ID NO: 2 , 4 , 8 , 106 , 252 , 446 , 482 , 516 , 618 , 714 , 830 , 894 , and/or 988 , or a functional fragment thereof , wherein said engineered phenylalanine ammonia lyase comprises at least one substitution or substitution set in said polypeptide sequence , and wherein the amino acid positions of said polypeptide sequence are numbered with reference to SEQ ID NO: 2 , 4 , 8 , 106 , 252 , 446 , 482 , 516 , 618 , 714 , 830 , 894 , 988 , and/or 1140 , respectively.2. The engineered phenylalanine ammonia lyase of claim 1 , wherein said engineered phenylalanine ammonia lyase comprises a polypeptide sequence having at least 85% claim 1 , 86% claim 1 , 87% claim 1 , 88% claim 1 , 89% claim 1 , 90% claim 1 , 91% claim 1 , 92% claim 1 , 93% claim 1 , 94% claim 1 , 95% claim 1 , 96% claim 1 , 97% claim 1 , 98% claim 1 , 99% claim 1 , or more sequence identity to SEQ ID NO: 4 claim 1 , or a functional fragment thereof claim 1 , and wherein said engineered phenylalanine ammonia lyase comprises at least one substitution or substitution set at one or more positions selected from 80/99/104/175/220/359 claim 1 , 80/104 claim 1 , 80/104/105/172 claim 1 , 80/104/105/172/175/222/359 claim 1 , 80/104/105/172/220/222 claim 1 , 80/104/105/220 claim 1 , 80/104/105/220/222/416 claim 1 , 80/104/105/222 claim 1 ...

Tissue specific reduction of lignin

The present invention provides an expression cassette comprising a polynucleotide that encodes a protein that diverts a monolignol precursor from a lignin biosynthesis pathway in the plant, which is operably linked to a heterologous promoter. Also provided are methods of engineering a plant having reduced lignin content, as well as plant cells, plant parts, and plant tissues from such engineered plants.

COMPOSITIONS AND METHODS FOR PROMOTING NEURONAL OUTGROWTH

Neural outgrowth in the central nervous system is achieved by administering chondroitinase AC and/or chondroitinase B to degrade chondroitin sulfate proteoglycans that inhibit or contribute to the inhibition of nervous tissue regeneration. 1. A method of treating a subject having an injury to the central nervous system comprising administering an effective amount of chondroitinase AC , chondroitinase B , or a mixture thereof to the subject.212-. (canceled)13. A method of promoting neurite outgrowth in a subject comprising administering an effective amount of chondroitinase AC , chondroitinase B , or a mixture thereof to the subject.1426-. (canceled) This application is a continuation application of U.S. application Ser. No. 10/513,573, with a filing date of Mar. 7, 2006, which is an national phase application filed under 35 U.S.C. §371 of International Appln. No. PCT/US03/14156, filed May 5, 2003, which claims priority to U.S. Provisional Appln. No. 60/377,669, filed May 4, 2002, the contents of each being incorporated by reference as if set forth in their entirely herein.1. Technical FieldThis disclosure relates to methods for promoting neurite outgrowth after nerve cell loss as a result of central nervous system (“CNS”) injury or disease. In particular, chondroitinase AC and chondroitinase B are used to promote neurite outgrowth.2. Description of Related ArtAfter a spinal cord injury in the adult mammalian central nervous system (CNS), the inability of axons to regenerate may lead to permanent paralysis. An injury-caused lesion will develop glial scarring, which contains extracellular matrix molecules including chondroitin sulfate proteoglycans (CSPGs). CSPGs inhibit nerve tissue growth in vitro, and nerve tissue regeneration at CSPGs rich regions in vivo.A number of molecules, and specified regions thereof, have been implicated in the ability to support the sprouting of neurites from a neuronal cell, a process also referred to as neurite outgrowth. The term ...

INTEGRATED PROCESS FOR DUAL BIOCATALYTIC CONVERSION OF CO2 GAS INTO BIO-PRODUCTS BY ENZYME ENHANCED HYDRATION AND BIOLOGICAL CULTURE

A method, process, apparatus, use and formulation for dual biocatalytic conversion of COcontaining gas into carbon containing bio-products by enzymatic hydration of COinto bicarbonate ions in the presence of carbonic anhydrase and metabolic conversion of the bicarbonate ions into carbon containing bio-products in a biological culture. The dual biocatalytic conversion may be relatively constant with controlling a feeding of the bicarbonate ions to the biological culture in accordance with demands of the biological culture by retaining over-production of bicarbonate ions and feeding part of the over-production to the biological culture in accordance with nutrient demands of the biological culture. Bicarbonate ions may also be reconverted to generate a pure COgas stream. The COcontaining gas may be derived from operations of a power plant which receives a carbon-containing fuel for combustion, and the biological culture may be an algae culture. 174-. (canceled)75. A method for dual biocatalytic conversion of COin a COcontaining gas into carbon containing bio-products by enzymatically catalyzing the hydration reaction of dissolved COinto bicarbonate and hydrogen ions in the presence of carbonic anhydrase and metabolically converting the bicarbonate ions into the carbon containing bio-products in a biological culture.76. The method of claim 75 , comprising maintaining the dual biocatalytic conversion relatively constant and controlling a feeding of the bicarbonate ions to the biological culture in accordance with demands of the biological culture by retaining over-production of bicarbonate ions and feeding part of the over-production to the biological culture in accordance with nutrient demands of the biological culture.77. The method of claim 76 , wherein the over-production of the bicarbonate ions is retained in the form of carbonate precipitates.78. A process for treating a COcontaining gas to produce carbon containing bio-products claim 76 , comprising:{'sub': '2', ' ...

NUCLEIC ACID, FUSION PROTEIN, RECOMBINED CELL, AND ISOPRENE OR CYCLIC TERPENE PRODUCTION METHOD

Provided is a nucleic acid encoding a fusion protein, the fusion protein including a first protein selected from the group consisting of isoprene synthase and cyclic terpene synthase, and a FKBP family protein linked to the first protein. Provided is a fusion protein encoded by the nucleic acid. Provided is a recombinant cell including the nucleic acid and expressing the fusion protein. Further provided is a recombinant cell including a first nucleic acid encoding the first protein and a second nucleic acid encoding the FKBP family protein, and expressing the first protein and the FKBP family protein. As a host cell, a syngas-assimilating bacterium or a methanol assimilating bacterium can be used. 1. A nucleic acid encoding a fusion protein , the fusion protein comprising:a first protein selected from the group consisting of isoprene synthase and cyclic terpene synthase; anda FKBP family protein linked to the first protein.2. The nucleic acid according to claim 1 , wherein the first protein is isoprene synthase.3. The nucleic acid according to claim 2 , wherein the isoprene synthase is any one of the following (a-1) to (a-3):(a-1) a protein consisting of the amino acid sequence of SEQ ID NO: 2,(a-2) a protein consisting of the amino acid sequence in which 1 to 20 amino acids are deleted, substituted or added in the amino acid sequence of SEQ ID NO: 2, and having isoprene synthase activity, and(a-3) a protein consisting of an amino acid sequence having homology of 90% or more with the amino acid sequence of SEQ ID NO: 2, and having isoprene synthase activity.4. The nucleic acid according to claim 1 , wherein the first protein is cyclic monoterpene synthase.5. The nucleic acid according to claim 4 , wherein the cyclic monoterpene synthase is phellandrene synthase.6. The nucleic acid according to claim 4 , wherein the cyclic monoterpene synthase is any one of the following (b-1) to (b-3):(b-1) a protein consisting of the amino acid sequence of SEQ ID NO: 4,(b-2) a ...

COMPOSITIONS AND METHODS OF USING CHONDROITINASE ABCI MUTANTS

The present disclosure relates to protein and nucleic acid mutants of chondroitinase ABCI. Such nucleic acid mutants encode for chondroitinase ABCI mutant enzymes exhibiting altered chondroitin lyase activity or increased resistance to inactivation from stressors including UV light or heat. Methods of using such nucleic acid mutants encoding chondroitinase ABCI mutant enzymes is also provided. 1. A pharmaceutical composition comprising an effective amount of mutant chondroitinase ABC I enzyme selected from SEQ ID NO: 1 , SEQ ID NO: 2 , SEQ ID NO: 5 , SEQ ID NO:6 , and combinations thereof , and a pharmaceutically acceptable carrier or diluent.2. The pharmaceutical composition of claim 1 , wherein the composition comprises mutant chondroitinase ABC I enzyme SEQ ID NO: 1.3. The pharmaceutical composition of claim 1 , wherein the composition comprises mutant chondroitinase ABC I enzyme SEQ ID NO: 2.4. The pharmaceutical composition of claim 1 , wherein the composition comprises mutant chondroitinase ABC I enzyme SEQ ID NO: 5.5. The pharmaceutical composition of claim 1 , wherein the composition comprises mutant chondroitinase ABC I enzyme SEQ ID NO: 6.6. The pharmaceutical composition of claim 1 , wherein the composition is a sustained release composition.7. A pharmaceutical composition comprising an effective amount of a nucleic acid sequence encoding for a mutant chondroitinase ABC I enzyme claim 1 , wherein the nucleic acid sequence is selected from SEQ ID NO: 9 claim 1 , SEQ ID NO: 10 claim 1 , SEQ ID NO: 13 claim 1 , SEQ ID NO:14 claim 1 , and combinations thereof claim 1 , and a pharmaceutically acceptable carrier or diluent.8. The pharmaceutical composition of claim 7 , wherein the composition comprises the nucleic acid sequence of SEQ ID NO: 9.9. The pharmaceutical composition of claim 7 , wherein the composition comprises the nucleic acid sequence of SEQ ID NO: 10.10. The pharmaceutical composition of claim 7 , wherein the composition comprises the nucleic ...

METHODS OF TREATING NEURODEGENERATIVE CONDITIONS

The present disclosure is directed to adeno-associated viral vector monoclonal antibody constructs and compositions thereof, methods of improving locomotor function after spinal cord injury, methods of treating neurodegenerative diseases. 1. An adeno-associated viral vector monoclonal antibody construct AAV10-NG2Ab of SEQ ID NO. 1.2. A method of improving locomotor function after spinal cord injury in a subject in need thereof comprising the administration of AAV10-NG2Ab and a pharmaceutically acceptable carrier.3. The method of any wherein said administration is intraspinal.4. The method of claim 2 , wherein the AAV10-NG2Ab is administered in an amount of about 1.0×10to about 8.0×10GC/mL.5. The method of claim 2 , wherein the AAV10-NG2Ab is administered in an amount of about 6.8×10GC/mL.6. The method of claim 2 , wherein the administration occurs for about one day to about ten weeks claim 2 ,7. The method of claim 2 , wherein the administration occurs for about one week to about five weeks.8. The method of claim 2 , wherein the administration occurs for about two weeks to about four weeks.9. A composition claim 2 , the composition comprising a therapeutically effective amount of AAV10-NG2Ab and at least one of a pharmaceutically acceptable carrier claim 2 , diluent and excipient.10. A method of treating neurodegenerative disease in a subject in need thereof comprising the administration of at least one adeno-associated virus selected from the group consisting of AAV-1 claim 2 , AAV-5 claim 2 , AAV-9 claim 2 , AAV-rh10 and AAV-hu11 and a pharmaceutically acceptable carrier.11. A method of improving locomotor function after spinal cord injury in a subject in need thereof comprising the administration of AAV-rh10-NT3/chondroitinase-ABC and a pharmaceutically acceptable carrier.12. A method of improving locomotor function after spinal cord injury in a subject in need thereof comprising the administration of AAV10-NT3 and a pharmaceutically acceptable carrier.13. A ...

ISOPRENE SYNTHASE AND GENE ENCODING THE SAME, AND METHOD FOR PRODUCING ISOPRENE MONOMER

The present invention provides means useful for establishing an excellent isoprene monomer production system. Specifically, the present invention provides a polynucleotide of the following (a), (b), or (c): 1. A polynucleotide of the following (a) , (b) , or (c):(a) a polynucleotide comprising (i) the nucleotide sequence represented by SEQ ID NO:1, or (ii) the nucleotide sequence consisting of the nucleotide residues at positions 133 to 1785 in the nucleotide sequence represented by SEQ ID NO:1;(b) a polynucleotide that comprises a nucleotide sequence having 90% or more identity to the nucleotide sequence of (i) or (ii), and encodes a protein having an isoprene synthase activity; or(c) a polynucleotide that hybridizes under a stringent condition with a polynucleotide consisting of the nucleotide sequence complementary to the nucleotide sequence of (i) or (ii), and encodes a protein having an isoprene synthase activity.2Mucuna.. The polynucleotide according to claim 1 , wherein the polynucleotide is derived from3. A protein of the following (A) claim 1 , (B) claim 1 , or (C):(A) a protein comprising (i′) the full length amino acid sequence represented by SEQ ID NO:2, or (ii′) the amino acid sequence consisting of the amino acid residues at positions 45 to 594 in the amino acid sequence represented by SEQ OD NO:2;(B) a protein that comprises an amino acid sequence having 90% or more identity to the amino acid sequence of (i′) or (ii′), and has an isoprene synthase activity; or(C) a protein that comprises an amino acid sequence having a deletion, substitution, addition or insertion of one or several amino acids in the amino acid sequence of (i′) or (ii′), and has an isoprene synthase activity.4. An expression vector comprising the polynucleotide according to .5. A transformant prepared by introducing the expression vector according to into a host.6. The transformant according to claim 5 , wherein the host has an ability to synthesize dimethylallyl diphosphate via a ...

Methods and Compositions for PCR

A modified thermostable Pol B DNA polymerase, produced by a reaction, under essentially aqueous conditions, of a thermostable Pol B DNA polymerase and a modifier reagent of Formula I wherein the reaction results in a thermally reversible inactivation of the thermostable Pol B DNA polymerase activity and the 3′-5′ exonuclease activity, which polymerase is suitable for hot-start PCR. Also disclosed are the method for the modification, a polynucleic acid amplification method and PCR reaction mixture and kit comprising the modified thermostable Pol B DNA polymerase. 2. The modified thermostable Pol B DNA polymerase according to claim 1 , wherein the Pol B DNA polymerase is Pfu claim 1 , KOD claim 1 , Tli claim 1 , or Pfx claim 1 , or a DNA polymerase sold under the trade names Vent® claim 1 , Deep Vent® claim 1 , Phusion™ claim 1 , or iProof™ claim 1 , or a fragment or variant thereof having DNA polymerase activity and 3′-5′ exonuclease activity.3. The modified thermostable Pol B DNA polymerase according to claim 1 , wherein the Pol B DNA polymerase is a fusion protein comprises Pfu claim 1 , KOD claim 1 , Tli claim 1 , or Pfx claim 1 , or a DNA polymerase sold under the trade names Vent® claim 1 , Deep Vent® claim 1 , Phusion™ claim 1 , or iProof™ claim 1 , or a fragment or variant thereof having DNA polymerase activity and 3′-5′ exonuclease activity.4. The modified thermostable Pol B DNA polymerase according to claim 1 , wherein the Pol B DNA polymerase is a fusion protein which comprises Pfu.5. The modified thermostable Pol B DNA polymerase of claim 4 , wherein the Pol B DNA polymerase is 10His-Pfu-Pae3192.6. The modified thermostable Pol B DNA polymerase according to claim 1 , wherein the modifier reagent is selected from the group consisting of maleic anhydride or a substituted maleic anhydride.7. The modified thermostable Pol B DNA polymerase according to claim 1 , wherein the modifier reagent is citraconic anhydride claim 1 , cis-aconitic anhydride claim 1 , 2 ...

MODIFIED MICROORGANISMS AND METHODS OF MAKING BUTADIENE USING SAME

The present disclosure generally relates to microorganisms that comprise one or more polynucleotides coding for enzymes in one or more pathways that catalyze a conversion of a fermentable carbon source to butadiene. Also provided are methods of using the microorganisms in industrial processes including, for use in the production of butadiene and products derived therefrom. 1. A method for producing butadiene , the method comprising: catalyzing a conversion of crotonyl alcohol to butadiene with an enzyme having an amino acid sequence at least 70% identical to linalool dehydratase (GI: 302064203).2. The method of claim 1 , wherein the enzyme is at least 80% identical to linalool dehydratase (GI: 302064203).3. The method of claim 1 , wherein the enzyme is at least 95% identical to linalool dehydratase (GI: 302064203).4. The method of claim 1 , wherein the enzyme is linalool dehydratase (GI: 302064203).5. The method of claim 1 , wherein the enzyme accepts crotonyl alcohol as a substrate.6. The method of claim 1 , wherein the enzyme has dehydratase activity.7. The method of claim 1 , wherein the enzyme has isomerase activity8. The method of claim 1 , wherein the enzyme has dehydratase and isomerase activity.9. The method of claim 1 , wherein the method is performed in a microorganism.10. A method for producing butadiene claim 1 , the method comprising: catalyzing a conversion of crotonyl alcohol to butadiene with an enzyme having an amino acid sequence at least 70% identical to a linalool dehydratase (EC 4.2.1.127).11. The method of claim 10 , wherein the enzyme is at least 80% identical to a linalool dehydratase (EC 4.2.1.127).12. The method of claim 10 , wherein the enzyme is at least 95% identical to a linalool dehydratase (EC 4.2.1.127).13. The method of claim 10 , wherein the enzyme is a linalool dehydratase (EC 4.2.1.127).14. The method of claim 10 , wherein the enzyme accepts crotonyl alcohol as a substrate.15. The method of claim 10 , wherein the enzyme has ...

Production of Alkenes by Combined Enzymatic Conversion of 3-Hydroxyalkanoic Acids

The present invention relates to a method for generating alkenes through a biological process. More specifically, the invention relates to a method for producing alkenes (for example propylene, ethylene, 1-butylene, isobutylene or isoamylene) from molecules of the 3-hydroxyalkanoate type. 119-. (canceled)20. A method for producing an alkene comprising the conversion of a 3-hydroxyalkanoate into said alkene by:(i) a first enzyme having an activity of converting the 3-hydroxyalkanoate into the corresponding 3-phosphonoxyalkanoate; and(ii) a second enzyme being different from the first enzyme and having an activity of converting said 3-phosphonoxyalkanoate into said alkene.21. The method of claim 20 , wherein the first enzyme is a mevalonate diphosphate (MDP) decarboxylase and the second enzyme is a different mevalonate diphosphate (MDP) decarboxylase.22. The method of wherein: (A) a protein comprising the amino acid sequence as shown in SEQ ID NO: 1 or a protein comprising an amino acid sequence which is at least 75% identical to the amino acid sequence shown in SEQ ID NO: 1 and showing an activity of converting the 3-hydroxyalkanoate into the corresponding 3-phosphonoxyalkanoate which is at least as high as the corresponding activity of the protein having the amino acid sequence shown in SEQ ID NO: 1;', '(B) a protein comprising the amino acid sequence as shown in SEQ ID NO: 2 or a protein comprising an amino acid sequence which is at least 75% identical to the amino acid sequence shown in SEQ ID NO: 2 and showing an activity of converting the 3-hydroxyalkanoate into the corresponding 3-phosphonoxyalkanoate which is at least as high as the corresponding activity of the protein having the amino acid sequence shown in SEQ ID NO: 2;', '(C) a protein comprising the amino acid sequence as shown in SEQ ID NO: 3 or a protein comprising an amino acid sequence which is at least 75% identical to the amino acid sequence shown in SEQ ID NO: 3 and showing an activity of ...

Polypeptide Assemblies and Methods for the Production Thereof

The application discloses multimeric assemblies including multiple oligomeric substructures, where each oligomeric substructure includes multiple proteins that self-interact around at least one axis of rotational symmetry, where each protein includes one or more polypeptide-polypeptide interface (“O interface”); and one or more polypeptide domain that is capable of effecting membrane scission and release of an enveloped multimeric assembly from a cell by recruiting the ESCRT machinery to the site of budding by binding to one or more proteins in the eukaryotic ESCRT complex (“L domain”); and where the multimeric assembly includes one or more subunits comprising one or more polypeptide domain that is capable of interacting with a lipid bilayer (“M domain”), as well as membrane-enveloped versions of the multimeric assemblies. 1. A multimeric assembly , comprising a plurality of oligomeric substructures , wherein each oligomeric substructure comprises a plurality of proteins that self-interact around at least one axis of rotational symmetry , wherein each protein comprises:(a) one or more polypeptide-polypeptide interface (“O interface”);(b) one or more polypeptide domain that is capable of effecting membrane scission and release of an enveloped multimeric assembly from a cell by recruiting the ESCRT machinery to the site of budding by binding directly or indirectly to one or more ESCRT or ESCRT-associated proteins (“L domain”);wherein the multimeric assembly comprises one or more polypeptide domain that is capable of interacting with a lipid bilayer (“M domain”);wherein the M domain, L domain, and O interface are not each present in a single naturally occurring protein, wherein the plurality of oligomeric substructures interact with each other at the one or more O interfaces.2. The multimeric assembly of claim 1 , wherein each oligomeric structure comprises one or more M domain claim 1 , or wherein each protein comprises one or more M domain.3. The multimeric assembly ...

NOVEL LYSINE DECARBOXYLASE, AND METHOD FOR PRODUCING CADAVERINE BY USING SAME

The present invention relates to: a novel lysine decarboxylase; a microorganism transformed with a gene coding for the activity concerned; and a method for producing cadaverine by using the same. 1. A protein having lysine decarboxylase activity , comprising an amino acid sequence of SEQ ID NO: 1 or an amino acid sequence having 75% or more homology therewith.2. The protein having the lysine decarboxylase activity of claim 1 , where the amino acid sequence having 75% or more sequence homology is an amino acid sequence of SEQ ID NO: 3 claim 1 , 5 claim 1 , 7 claim 1 , or 9.3. A polynucleotide encoding the protein having the lysine decarboxylase activity of .4. The polynucleotide of claim 3 , wherein the polynucleotide has a nucleotide sequence of SEQ ID NO: 2 or a nucleotide sequence having 75% or more sequence homology therewith.5. The polynucleotide of claim 3 , wherein the nucleotide sequence having 75% or more sequence homology is a nucleotide sequence of SEQ ID NO: 2 claim 3 , 4 claim 3 , 8 claim 3 , or 10.6. A microorganism which is transformed to express the protein having the lysine decarboxylase activity of .7Escherichia. The microorganism of claim 6 , wherein the microorganism is an sp. microorganism.8. A microorganism having an ability to produce cadaverine claim 1 , wherein the microorganism having improved ability to produce lysine compared to a wild-type is transformed to express the protein having the lysine decarboxylase activity of .9EscherichiaCoryneform. The microorganism having an ability to produce cadaverine of claim 8 , wherein the microorganism is an sp. microorganism or a microorganism.10. A method of preparing cadaverine claim 8 , comprising the steps of:{'claim-ref': [{'@idref': 'CLM-00001', 'claim 1'}, {'@idref': 'CLM-00006', 'claim 6'}], 'converting lysine into cadaverine by using the protein having the lysine decarboxylase activity of or the microorganism of ; and'}recovering the converted cadaverine.11. A method of preparing cadaverine ...

OPTIMIZATION OF YEAST HOST CELLS FOR THE PRODUCTION OF HETEROLOGOUS PROTEINS

The present disclosure concerns yeast host cell especially suited for the expression of heterologous proteins, such as heterologous enzymes. The yeast host cell of the present disclosure exhibits an alteration in the cAMP signaling pathway which allows achieving increased heterologous protein yield and associated biological activity. The yeast host cell can also exhibit polyploidy. 1. A recombinant yeast host cell for making an increased amount of an heterologous protein , the recombinant yeast host cell:(i) has a first heterologous nucleic acid encoding the heterologous protein and an altered intracellular cyclic AMP (cAMP) signaling pathway; and/or(ii) is obtained by introducing the first heterologous nucleic acid in an ancestral yeast host cell having the altered intracellular cAMP pathway;wherein the altered intracellular cAMP pathway provides to the recombinant yeast host cell or the ancestral yeast host cell a substantially similar intracellular cAMP production in the presence and in the absence of a cAMP stimulus known to stimulate intracellular cAMP production in a control yeast cell.2. The recombinant yeast host cell of claim 1 , wherein the amount of heterologous protein per cell of the recombinant yeast host cell is increased with respect to a corresponding amount in a control yeast cell.3. The recombinant yeast host cell of or claim 1 , wherein the control yeast cell corresponds to biological deposit PTA-125176 or a yeast cell having the characteristics of the biological deposit PTA-125176.4. The recombinant yeast host cell of any one of to expressing a variant protein of the cAMP signaling pathway.5. The recombinant yeast host cell of claim 4 , wherein the variant protein is a variant CYR1 protein encoded by a variant CYR1 gene.6. The recombinant yeast host cell of claim 5 , wherein the variant CYR1 gene is a native CYR1 gene.7. The recombinant yeast host cell of any one of to claim 5 , wherein the ancestral yeast host cell is biological deposit PTA- ...

HERBICIDE-RESISTANT RICE PLANTS, POLYNUCLEOTIDES ENCODING HERBICIDE-RESISTANT ACETOHYDROXYACID SYNTHASE LARGE SUBUNIT PROTEINS, AND METHODS OF USE

The present disclosure provides a method for treating rice. The method comprises the steps of: providing a domestic rice crop plant and at least one AHAS-inhibiting herbicide selected from the group comprising a sulfonylurea herbicide, a sulfonyl carboxamide herbicide, an imidazolinone herbicide, a triazolopyrimidine herbicide, a pyrimidinyloxybenzoate herbicide, and a sulfonylaminocarbonyltriazolinone herbicide; applying an effective amount (measured in g Al/Ha) of one or more of the aforementioned herbicide to the domestic rice crop plant, post-emergence; thereby creating a treated rice plant; and growing the resulting treated rice plant. 1. A method for treating rice , comprising:providing a rice crop plant and at least one sulfonylurea herbicide;applying an effective amount of the at least one sulfonylurea herbicide to the rice crop plant, post-emergence; thereby creating a treated rice plant; andgrowing the resulting treated rice plant.2. The method of claim 1 , further comprising harvesting seed from the treated rice plant.3. The method of or claim 1 , wherein the rice crop plant comprises an acetohydroxyacid synthase large subunit (AHASL) polynucleotide encoding a herbicide-tolerant AHASL polypeptide comprising a leucine substitution at a position corresponding to position 171 of SEQ ID NO:26.4. The method of any one of - claim 1 , wherein the rice crop plant comprises an AHASL polypeptide comprising a leucine substitution at the position corresponding to position 171 of SEQ ID NO:26.5. The method of any one of - claim 1 , wherein the rice crop plant comprises the herbicide tolerance characteristics of a plant of line IMINTA 15.6. The method of any one of - claim 1 , wherein the rice crop plant:(a) is a plant of line IMINTA 15;(b) is a progeny of a plant of line IMINTA 15;(c) is a mutant or recombinant plant of line IMINTA 15; or(d) is a progeny of any one of the plants of (a)-(c).7. The method of claim 1 , wherein the sulfonylurea herbicide comprises one or ...

ENGINEERED PHENYLALANINE AMMONIA LYASE POLYPEPTIDES

The present invention provides engineered phenylalanine ammonia-lyase (PAL) polypeptides and compositions thereof, as well as polynucleotides encoding the engineered phenylalanine ammonia-lyase (PAL) polypeptides. 1. An engineered polynucleotide encoding an engineered polypeptide comprising an amino acid sequence having at least 90% sequence identity to reference sequence SEQ ID NO:4 , wherein said amino acid sequence comprises an amino acid residue selected from leucine , methionine , and glutamine at position 305 , wherein said positions in said amino acid sequence are in reference to SEQ ID NO:4.2. The engineered polynucleotide encoding the engineered polypeptide of claim 1 , wherein said engineered polypeptide exhibits an improved property selected from reduced sensitivity to proteolysis claim 1 , increased tolerance to acidic pH claim 1 , reduced immunogenicity claim 1 , or a combination thereof claim 1 , as compared to the reference sequence SEQ ID NO:4.3. The engineered polynucleotide encoding the engineered polypeptide of claim 2 , wherein the improved property is selected from reduced sensitivity to proteolysis and/or increased tolerance to acidic pH.4. The engineered polynucleotide encoding the engineered polypeptide of claim 1 , wherein said engineered polypeptide is resistant to proteolysis claim 1 , acid stable claim 1 , and/or deimmunized.5. The engineered polynucleotide encoding the engineered polypeptide of claim 4 , wherein said engineered polypeptide is resistant to proteolysis by at least one digestive tract enzyme claim 4 , wherein said engineered polypeptide is resistant to proteolysis by chymotrypsin claim 4 , trypsin claim 4 , carboxypeptidases claim 4 , and/or elastases.6. The engineered polynucleotide encoding the engineered polypeptide of claim 5 , wherein said engineered polypeptide is deimmunized.7. The engineered polynucleotide encoding the engineered polypeptide of claim 1 , wherein said polypeptide is purified.8. The engineered ...

ENGINEERED PHENYLALANINE AMMONIA LYASE POLYPEPTIDES

The present invention provides engineered phenylalanine ammonia-lyase (PAL) polypeptides and compositions thereof, as well as polynucleotides encoding the engineered phenylalanine ammonia-lyase (PAL) polypeptides. 1. An engineered polypeptide comprising an amino acid sequence having at least 90% sequence identity to reference sequence SEQ ID NO:12 , wherein said amino acid sequence comprises an amino acid residue selected from leucine , methionine , and glutamine at position 305 , and wherein said engineered polypeptide further comprises at least one or more of the following substitutions or substitution sets selected from 18 , 18/47 , 18/47/214 , 18/47/214/308 , 18/47/214/308/450/546 , 18/47/214/450 , 18/47/214/467/540/546 , 18/47/214/540 , 18/47/214/546 , 18/47/308/546 , 18/47/450 , 18/47/450/528/546 , 18/47/450/546 , 18/214 , 18/214/308 , 18/214/308/450/467 , 18/214/450 , 18/214/460 , 18/214/467/546 , 18/214/540 , 18/450/540 , 18/540 , 47 , 47/214 , 47/214/308 , 47/214/540 , 47/214/546 , 47/450 , 59/134 , 59/134/240/304/353/521/564 , 59/134/240/353 , 59/134/240/521 , 59/134/240/521/564 , 59/134/240/521/565 , 59/134/304/353/521 , 59/134/353/509/521 , 59/134/509 , 59/240 , 59/240/353/509 , 59/240/353/564/565 , 59/240/509/521/564 , 59/353 , 59/353/509/564 , 59/353/521 , 59/353/565 , 59/509/564 , 59/521 , 59/564 , 134/240/304/353/564 , 134/240/353/509/521/564 , 134/240/353/521/564 , 134/240/509/521 , 134/304/353/521/565 , 134/353/509/564 , 134/353/521 , 134/353/521/564 , 134/353/564 , 134/521 , 214/308/460 , 214/450/528 , 214/540 , 214/546 , 240 , 240/304/353/509/521/564 , 240/304/509 , 240/304/509/521 , 240/353/509 , 240/353/509/521 , 240/353/509/521/564/565 , 240/353/521 , 240/509 , 240/509/564/565 , 240/509/565 , 240/521/564/565 , 304/353/509 , 304/509 , 308/450/467 , 353/521 , 521 , and 528/546 , wherein said positions in said amino acid sequence are in reference to SEQ ID NO:12.2. The engineered polypeptide of claim 1 , wherein said engineered polypeptide ...

ENGINEERED PHENYLALANINE AMMONIA LYASE POLYPEPTIDES

The present invention provides engineered phenylalanine ammonia-lyase (PAL) polypeptides and compositions thereof, as well as polynucleotides encoding the engineered phenylalanine ammonia-lyase (PAL) polypeptides. 1. An engineered polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 90% sequence identity to reference sequence SEQ ID NO:24 , wherein said polypeptide comprises a mutation at position 509 , wherein said positions are numbered with reference to SEQ ID NO: 24.2. The engineered polynucleotide of claim 1 , wherein said encoded engineered polypeptide further comprises at least one amino acid residue differences as compared to SEQ ID NO:24 claim 1 , wherein the amino acid residue differences are at one or more amino acid positions selected from 20 claim 1 , 24 claim 1 , 27 claim 1 , 39 claim 1 , 43 claim 1 , 45 claim 1 , 47 claim 1 , 54 claim 1 , 58 claim 1 , 59 claim 1 , 62 claim 1 , 70 claim 1 , 73 claim 1 , 80 claim 1 , 82 claim 1 , 91 claim 1 , 94 claim 1 , 98 claim 1 , 104 claim 1 , 105 claim 1 , 110 claim 1 , 112 claim 1 , 115 claim 1 , 117 claim 1 , 118 claim 1 , 119 claim 1 , 121 claim 1 , 123 claim 1 , 124 claim 1 , 125 claim 1 , 126 claim 1 , 127 claim 1 , 128 claim 1 , 129 claim 1 , 130 claim 1 , 131 claim 1 , 133 claim 1 , 134 claim 1 , 135 claim 1 , 139 claim 1 , 140 claim 1 , 141 claim 1 , 142 claim 1 , 143 claim 1 , 144 claim 1 , 145 claim 1 , 146 claim 1 , 147 claim 1 , 149 claim 1 , 150 claim 1 , 151 claim 1 , 153 claim 1 , 154 claim 1 , 156 claim 1 , 157 claim 1 , 158 claim 1 , 159 claim 1 , 172 claim 1 , 174 claim 1 , 175 claim 1 , 176 claim 1 , 177 claim 1 , 178 claim 1 , 180 claim 1 , 187 claim 1 , 191 claim 1 , 195 claim 1 , 199 claim 1 , 205 claim 1 , 206 claim 1 , 210 claim 1 , 212 claim 1 , 213 claim 1 , 214 claim 1 , 232 claim 1 , 240 claim 1 , 243 claim 1 , 245 claim 1 , 247 claim 1 , 248 claim 1 , 250 claim 1 , 256 claim 1 , 257 claim 1 , 266 claim 1 , 270 claim 1 , 275 claim 1 , 278 claim 1 , 279 ...