МИКРООРГАНИЗМЫ ДЛЯ ПОЛУЧЕНИЯ ПУТРЕСЦИНА И СПОСОБ ПОЛУЧЕНИЯ ПУТРЕСЦИНА С ИХ ИСПОЛЬЗОВАНИЕМ

Изобретение относится к биотехнологии, а именно к путресцин-продуцирующему микроорганизму и способу получения путресцина с его использованием. При этом путресцин-продуцирующий микроорганизм модифицирован так, что у него делетирована активность орнитинкарбамоилтрансферазы и белка, участвующего в экспорте глутамата (NCgl1221), по сравнению с их эндогенными активностями, и активность орнитиндекарбоксилазы (ODC) введена в микроорганизм. Изобретение позволяет получать путресцин с высокой степенью эффективности. 2 н. и 11 з.п. ф-лы, 3 ил., 8 табл., 5 пр.

Микроорганизм, имеющий повышенную продуктивность в отношении молочной кислоты, и способ получения молочной кислоты с использованием данного микроорганизма

Изобретение относится к области биохимии, генной инженерии и биотехнологии, в частности к модифицированному микроорганизму Saccharomyces cerevisiae, имеющему повышенную продуктивность в отношении молочной кислоты. Настоящий модифицированный микроорганизм характеризуется тем, что в нем снижена активность пируватдекарбоксилазы, усилены активности альдегиддегидрогеназы и ацетил-КоА-синтетазы и в него введена дегидрогеназа молочной кислоты. В результате указанных модификаций этот микроорганизм способен продуцировать молочную кислоту с высоким выходом. Изобретение также относится к способу получения молочной кислоты. Настоящий способ предусматривает культивирование указанного микроорганизма и выделение из культуральной среды молочной кислоты, продуцируемой при культивировании этого микроорганизма. Настоящее изобретение позволяет получать молочную кислоту с высоким выходом. 2 н. и 4 з.п. ф-лы, 1 ил., 14 табл., 10 пр.

ФЕРМЕНТАТИВНОЕ ПОЛУЧЕНИЕ ЧЕТЫРЕХУГЛЕРОДНЫХ СПИРТОВ

Изобретение относится к биотехнологии и представляет собой способ получения изобутанола, включающий получение рекомбинантной микробной клетки-хозяина, содержащей ферментативный путь изобутанола, включающий молекулы ДНК, кодирующие набор полипептидов, которые катализируют следующие превращения субстрата в продукт: i) пирувата в ацетолактат; ii) ацетолактата в 2,3-дигидроксиизовалерат; iii) 2,3-дигидроксиизовалерата в α-кетоизовалерат; iv) α-кетоизовалерата в изобутиральдегид; и v) изобутиральдегида в изобутанол, и контактирование клетки-хозяина с ферментируемым углеродным субстратом в среде ферментации в условиях, при которых продуцируется изобутанол. Изобретение позволяет получать изобутанол с высокой степенью эффективности. 3 н. и 51 з.п. ф-лы, 1 ил., 13 табл.

СПОСОБ ПОЛУЧЕНИЯ L-АМИНОКИСЛОТЫ С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ, ПРИНАДЛЕЖАЩЕЙ К РОДУ Escherichia

Изобретение относится к биотехнологии и предоставляет собой способ получения L-аминокислоты с использованием бактерии, принадлежащей к роду Escherichia, которая модифицирована таким образом, что экспрессия гена ydbK в указанной бактерии усилена. Изобретение позволяет получать L-аминокислоты с высокой степенью эффективности. 2 н.и 7 з.п. ф-лы, 2 ил, 3 табл.

СПОСОБ ПОЛУЧЕНИЯ L-АРГИНИНА С ИСПОЛЬЗОВАНИЕМ БАКТЕРИЙ РОДА Escherichia, В КОТОРОЙ ИНАКТИВИРОВАН ОПЕРОН astCADBE

Настоящее изобретение относится к биотехнологии и представляет собой способ получения L-аргинина с использованием бактерии, принадлежащей к роду Escherichia, которая модифицирована таким образом, что оперон astCADBE в указанной бактерии инактивирован. Указанную бактерию выращивают в питательной среде, после чего L-аргинин выделяют из культуральной жидкости. Данный способ позволяет повысить продуктивность бактерий-продуцентов L-аргинина и получить L-аргинин с большим выходом. 2 н. и 2 з.п. ф-лы, 2 табл., 14 пр.

Микроорганизмы, продуцирующие L-валин, и способ получения L-валина с их использованием

Изобретение относится к биотехнологии. Предложен микроорганизм, продуцирующий L-валин, обладающий усиленной активностью дегидратазы дигидроксикислоты по сравнению с эндогенной активностью. Также микроорганизм обладает любой одной или более чем одной из комбинаций, выбранных из уменьшенной активности трансаминазы C по сравнению с эндогенной активностью, ослабленной активности пируватдегидрогеназы по сравнению с эндогенной активностью и ослабленной активности цитратсинтазы по сравнению с эндогенной активностью. Предложен также способ получения L-валина с использованием указанного микроорганизма. Изобретение обеспечивает получение L-валина с высоким выходом. 2 н. и 13 з.п. ф-лы, 11 табл., 2 пр.

ПОЛУЧЕНИЕ ЖИРНЫХ СПИРТОВ С ПОМОЩЬЮ ОБРАЗУЮЩИХ ЖИРНЫЕ СПИРТЫ АЦИЛ-КОА-РЕДУКТАЗ (FАR)

... 1. Способ получения композиции жирных спиртов, включающий в себя:a) культивирование рекомбинантного микроорганизма в подходящей культуральной среде, где рекомбинантный микроорганизм содержит ген, кодирующий гетерологичный фермент редуктазу жирных ацилов (FAR), обладающий по меньшей мере 75% идентичностью последовательности (по меньшей мере 80%, по меньшей мере 85%, по меньшей мере 90% и по меньшей мере 95% идентичностью последовательности) с SEQ ID NO: 2, SEQ ID NO: 6, SEQ ID NO: 14, или их функциональными фрагментами, иb) обеспечение экспрессии указанного гена, где указанная экспрессия приводит к получению композиции жирных спиртов.2. Способ по п.1, где фермент FAR обладает по меньшей мере 85% идентичностью последовательности (по меньшей мере 90% и по меньшей мере 95% идентичностью последовательности) с SEQ ID NO: 2 или ее функциональными фрагментами.3. Способ по п.1, где фермент FAR содержит последовательность из SEQ ID NO: 2, SEQ ID NO: 6, SEQ ID NO: 14 или их функциональные фрагменты ...

МИКРООРГАНИЗМЫ, ИМЕЮЩИЕ УЛУЧШЕННУЮ ОРНИТИН-ПРОДУЦИРУЮЩУЮ СПОСОБНОСТЬ, И СПОСОБ ПОЛУЧЕНИЯ ОРНИТИНА С ИХ ИСПОЛЬЗОВАНИЕМ

... 1. Микроорганизм, имеющий улучшенную орнитин-продуцирующую способность, где активности орнитинкарбамоилтрансферазы и белка, участвующего в экспорте глутамата (NCgl1221), модифицированы таким образом, что они являются аттенуированными в сравнении с их эндогенными активностями.2. Микроорганизм по п. 1, где орнитинкарбамоилтрансфераза имеет аминокислотную последовательность SEQ ID NO:18 или аминокислотную последовательность, имеющую 70% или более высокую гомологию с этой последовательностью.3. Микроорганизм по п. 1, где белок, участвующий в экспорте глутамата, имеет аминокислотную последовательность SEQ ID NO:20 или аминокислотную последовательность, имеющую 70% или более высокую гомологию с этой последовательностью.4. Микроорганизм по п. 1, где активность орнитинкарбамоилтрансферазы и белка, участвующего в экспорте глутамата, является аттенуированной способом, выбранным из группы, состоящей из (1) частичной или полной делеции гена, кодирующего этот белок, (2) модификации регуляторной последовательности ...

METHYLOTROPHE HEFE,DIE EINE ZUCKERKETTE EINES SÄUGERS HERSTELLT

VERFAHREN ZUR REINIGUNG UND GEGEBENENFALLS GEWINNUNG VON FORMIAT-DEHYDROGENASE (FDH) AUS CANDIDA BOIDINII UND FDH-HALTIGES PRODUKT.

In a new process for the purificn. and optional recovery of formate dehydrogenase (FDH) from Candida biodinii in which (1) the enzyme-contg. cells are digested, (2) a phase partition (affinity extraction) is performed and (3) the enzyme is opt. sepd. from the phase in which it is enriched and opt. recovered, step 2 is carried out with an aq. 2-phase system one phase of which is enriched with a triazine dyestuff (ligand) bound to an inert water -sol. polymer, opt. without previously sepg. off cells and cell debris and/or of foreign proteins. Processes (esp. as defined above) are new when the Candida boidinii cells, after previous freezing, are suspended in an aq. phosphate-contg. medium and left in the suspension until enzyme extraction reaches not more than ca. 90, 85 or 75%, the resulting suspension opt. being subjected to the phase partition.

KONSTITUTIVE MAISPROMOTOREN

Mikrobiologische Herstellung von C4-Körpern aus Saccharose und Kohlendioxid

Die vorliegende Erfindung betrifft eine Zelle, die gegenüber ihrem Wildtyp derart gentechnisch verändert wurde, dass sie im Vergleich zu ihrem Wildtyp, aus Saccharose und Kohlendioxid als Kohlenstoffquelle, mehr C4-Körper und/oder mehr über diese C4-Körper hergestellte Folgeverbindungen zu bilden vermag. Die Erfindung betrifft ferner ein Verfahren zur Herstellung einer solchen gentechnisch veränderten Zelle und ein Verfahren zur Herstellung von C4-Körpern und/oder von über diese C4-Körper hergestellte Folgeverbindungen mit Hilfe dieser Zellen. Schließlich betrifft die Erfindung noch die Verwendung der Zellen zur Herstellung von C4-Körpern und/oder von über diese C4-Körper hergestellte Folgeverbindungen aus Saccharose und Kohlendioxid.

PROMOTOR/TERMINATOR DES FORMATDEHYDROGENASE-GENS VON CANDIDA BOIDINII

METHOD FOR QUANTITATIVE DETERMINATION OF POLYAMINES

Microorganism production of high-valve chemical products, and related compositions, methods and systems

New Process

Production of butanol

Production of butanol using thermophilic Bacillaceae

A process of producing butanol is disclosed comprising culturing a recombinant butanol-tolerant thermophilic Bacillaceae comprising one or more heterologous nucleic acid molecules which encode one or more butanol biosynthetic pathway enzymes selected from the group consisting of enzymes which catalyse one or more of the reactions butyryl-CoA to butyraldehyde, butyraldehyde to 1-butanol, crotonyl-CoA to butyryl-CoA, 3-hydroxybutyryl-CoA to crotonyl-CoA, acetoacetyl-CoA to 3-hydroxybutyryl-CoA, and acetyl-CoA to acetoacetyl-CoA. Methods for making recombinant thermophilic Bacillaceae bacteria comprising introducing nucleic acid molecules encoding one or more butanol biosynthetic pathway enzymes into the bacteria are also claimed, along with recombinant thermophilic Bacillaceae comprising these nucleic acid molecules. The thermophilic Bacillaceae are preferably Geobacillus or Ureibacillus. The enzymes of the butanol biosynthetic pathway may be acetaldehyde dehydrogenase or butyryl CoA dehydrogenase ...

Transgenic rice plant and its family with environmental stress resistant by proline accumulation of high level and its production

Modified cell

Cell

Enhancement of microbial ethanol production

Outer surface proteins, their genes, and their use.

Enhancement of microbial ethanol production

Repellent compositions containing aromatic aldehydes

Outer surface proteins, their genes, and their use.

Enhancement of microbial ethanol production

Enhancement of microbial ethanol production

Outer surface proteins, their genes, and their use.

POLYPEPTIDE WITH 4-CUMARATE: COA LEAGUE SE ACTIVITY AND THEIR USES.

PROCESS FOR THE PRODUCTION OF HPPD INHIBITOR HERBICIDE TOLERANT PLANZEN BY EVASION OF THE HPPD METABOLIC PATHWAY.

NUKLEINSÄURE-PROMOTOR

The present invention relates to a nucleic acid promoter comprising a sequence having at least 70% identity to SEQ ID No. 1 or a functional fragment thereof, or a sequence which hybridizes thereto under stringent conditions.

OXIDOREDUKTASEN ZUR STEREOSELEKTIVEN REDUKTION VON KETOVERBINDUNGEN

VERFAHREN ZUR ENANTIOSELEKTIVEN ENZYMATISCHEN REDUKTION VON HYDROXYKETOVERBINDUNGEN

PROCEDURE FOR THE PRODUCTION OF L-LYSIN

BIOLOGICAL SYSTEMS FOR the PRODUCTION OF POLYHYDROXYALKANOATE POLYMERS the 4-HYDROXYSÄURE CONTAINING

MOLECULAR DISPLAY ON MULTIMEREN PROTEIN STANDS, the OF of the E2 COMPONENT the ALPHA KETOSÄURE DEHYDROGENASE COMING

REKOMBINANTE AVIRULENTE SALMONELLA ANTI-FERTILITY VACCINES

BIFUNCTIONAL ENZYMES FOR BIO POLYMER PRODUCTION

REKOMBINANTE CORYNEFORMBAKTERIE THE GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE -2 ÜBEREXPRIMIEREN, AND PROCEDURE FOR THE PRODUCTION OF L-LYSINE

FOR A CINNAMOYL COA REDUKTASE CODING DNA SEQUENCES, AND YOUR USE FOR THE REGULARIZATION OF THE LIGNUN CONTENT OF PLANTS

Method for obtaining transgenic plants expressing a protein with activity producing hydrogen peroxide by transformation by (agrobacterium rhizogenes)

FUSION PROTEINS HAVING AN IN VIVO POST-TRANSLATIONAL MODIFICATION SITE AND METHODS OF MANUFACTURE AND PURIFICATION

Polynucleotides encoding lignin biosynthetic pathway enzymes in coffee

Metabolically engineered micro-organisms having reduced production of undesired metabolic products

Method for the enantioselective enzymatic reduction of hydroxyketo compounds

Thermophilic microorganisms for ethanol production

RECOMBINANT AVIRULENT SALMONELLA ANTIFERTILITY VACCINES

Improved yeast production host cells

Crabtree positive yeast cells that have endogenous expressed pyruvate decarboxylase genes inactivated and an engineered biosynthetic pathway utilizing pyruvate were found to have improved growth and product yield when glucose repression was reduced. These cells were able to grow in media containing a high glucose concentration.

Methods and apparatuses for purification

Isolated human enzyme proteins, nucleic acid molecules encoding human enzyme proteins, and uses thereof

Purified polypeptides involved in membrane biogenesis

COUPLED ENZYMATIC REACTION SYSTEM USING A FORMATE DEHYDROGENASE DERIVED FROM LESS THANIGREATER THANCANDIDA BOIDINIILESS THAN/IGREATER THAN

Hydrocarbon synthase gene, and use thereor

Provided is a hydrocarbon synthase gene coding a protein that has a new function with a superior ability to synthesize hydrocarbons such as alkane. The hydrocarbon synthase gene codes a protein which includes an amino acid sequence having the sequence motif represented by SEQ ID NO: 1, and which synthesizes, from an aldehyde compound, a hydrocarbon having one less carbon atom.

Production of acetyl-coenzyme a derived isoprenoids

Provided herein are compositions and methods for the heterologous production of acetyl-CoA-derived isoprenoids in a host cell. In some embodiments, the host cell is genetically modified to comprise a heterologous nucleotide sequence encoding an acetaldehyde dehydrogenase, acetylating (ADA, E.C. 1.2.1.10) and an MEV pathway comprising an NADH-using HMG-CoA reductase. In some embodiments, the host cell is genetically modified to comprise a heterologous nucleotide sequence encoding an ADA and an MEV pathway comprising an acetoacetyl-CoA synthase. In some embodiments, the genetically modified host cell further comprises one or more heterologous nucleotide sequences encoding a phosphoketolase and a phosphotransacetylase. In some embodiments, the genetically modified host cell further comprises a functional disruption of the native PDH-bypass. The compositions and methods described herein provide an energy-efficient yet redox balanced route for the heterologous production of acetyl-CoA-derived ...

Production of plants resistant to attacks of sclerotinia sclerotiorum by introducing a gene coding for an oxalate oxidase

Constitutive maize promoters

Formaldehyde dehydrogenase genes from methylotrophic yeasts

A novel polypeptide - quinoprotein reductase 7 and a polynucleotide encoding thesame

PYRUVATE OXIDASE

Molecular display on multimeric protein scaffolds

Synthetic promoters

OUTER SURFACE PROTEINS, THEIR GENES, AND THEIR USE

... ▓▓▓According to the present invention, a series of genes are identified in Group ▓B Streptococcus, the products of which may be located on the outer surface of ▓the organism. The genes, or functional fragments thereof, may be useful in the ▓preparation of therapeutics, e.g. vaccines for the immunisation of a patient ▓against microbial infection.▓ ...

ANTHER-SPECIFIC TAA1 GENES ENCODING FATTY ACYL CO-A REDUCTASES, AND USES THEREOF

The present invention provides isolated and purified polynucleotide sequences encoding fatty acyl Co-A reductase (FAR) enzymes derived from wheat, designated TAA1 genes. The invention encompasses genes that encode FAR enzymes that are useful in the production of transgenic plants and other organisms that comprise increased or otherwise altered levels of fatty alcohols. Such plants may have significant commercial value for the production of fatty alcohols for use in nutritional and pharmaceutical compositions. The invention also provides corresponding TAA1 anther-specific promoters, suitable for the expression of proteins other than FAR enzymes in the anthers and pollen cells of suitably transformed plants.

TRANSGENIC RICE PLANT AND ITS FAMILY WITH ENVIRONMENTAL STRESS RESISTANT BY PROLINE ACCUMULATION OF HIGH LEVEL AND ITS PRODUCTION

In order to obtain a transformed rice plant having an improved salinity tolerance level because of its enhanced proline accumulating ability, a P5CS (.DELTA.1- pyrroline-5-carboxylate (P5C) synthetase) gene of rice or a P5CS gene of Arabidopsis thanliana and the antisense (reverse DNA sequence-containing) gene of a ProDH (Proline dehydrogenase) are introduced into a rice plant by using a genetic engineering technology.

MATERIALS AND METHODS FOR THE MODIFICATION OF PLANT LIGNIN CONTENT

Novel isolated polynucleotides and polypeptides associated with the lignin biosynthetic pathway are provided, together with constructs including such sequences. Methods for the modulation of lignin content, lignin structure and lignin composition in target organisms are also disclosed, the methods comprising incorporating one or more of the polynucleotides of the present invention into the genome of a target organism.

PROCESS FOR THE ENANTIOSELECTIVE ENZYMATIC REDUCTION OF SECODIONE DERIVATIVES

The invention relates to a process for the enantioselective enzymatic reduction of secodione derivatives of general formula I (see formula I) wherein the ring structures comprise no, one or several heteroatoms, R1 is hydrogen or a C1-C4 alkyl group, R2 is hydrogen, a C1-C8 alkyl group or a protective group for OH known in prior art, such as an ester, R3 is hydrogen, a methyl group or a halide, the structural element (see above formula) represents a benzene ring or a C6 ring having 0, I or 2 C-C double bonds, a double bond is optionally included at positions 6/7 or 7/8, and the carbon at positions 1, 2, 4, 5, 6, 7, 8, 9, 11, 12 and 16 is independently substituted with hydrogen, a C1-C4 alkyl group, a halide or a phenyl group, wherein the secodione derivative is reduced with an oxidoreductase/ dehydrogenase in the presence of NADH or NADPH as a cofactor. According to the invention, the secodione derivative is used in the reaction batch at a concentration of >=10 g/l and the oxidized cofactor ...

PROCESS FOR MANUFACTURE OF PYRUVATE OXIDASE AND ITS USE FOR THE ANALYSIS AND KIT

Pyruvate oxidase is produced by a process which comprises culturing A pyruvate oxidase-producing microorganism belonging to the genus Pediococcus, Streptococcus or Aerococcus in a nutrient culture medium, and isolating the pyruvate oxidase thus produced from the culture. also provided by the invention disclosed herein is an analytical method for pyruvic acid in a sample containing pyruvic acid or a system which liberates this acid, which comprises treating said sample with a reaction system containing pyruvate oxidase, and measuring the consumed component or generated component.

PROMOTORS OF FILAMENTOUS FUNGI AND USE THEREOF

Novel vectors are disclosed for use in filamentous fungi such as Aspergillus sp. in particular, whereby protein coding regions may be inserted therein to achieve expression or expression followed by secretion of the coded protein from the host. Signal peptide sequences and promoter sequences valuable for this purpose are disclosed as are expression vectors containing coding regions native or foreign to the fungal host. In accordance with the invention, a filamentous fungus such as Aspergillus may be provided with foreign or natural coding regions associated with foreign or natural promoter sequences and optionally signal peptide sequences which can be used to control the expression and/or secretion of the proteins encoded by these coding regions.

GENES INVOLVED IN CYCLODODECANONE DEGRADATION PATHWAY

A 10 kb gene cluster has been isolated from Rhodococcus ruber SC1 comprising genes encoding enzymes useful for the synthesis of dodecanoic diacid from cyclododecanone and other cyclic intermediates. The six specific open reading frames have been identified that are associated with dodecanoic diacid biosynthesis. In addition to the expected substrates the enzymes of the instant invention have moderate specificity for C11-C15 compounds.

MATERIALS AND METHODS FOR THE ALTERATION OF ENZYME AND ACETYL COA LEVELS IN PLANTS

The present invention provides nucleic acid and amino acid sequences of acetyl CoA synthetase (ACS), plastidic pyruvate dehydrogenase (pPDH), ATP citrate lyase (ACL), Arabidopsis pyruvate decarboxylase (PDC), and Arabidopsis aldehyde dehydrogenase (ALDH), specifically ALDH-2 and ALDH-4. The present invention also provides a recombinant vector comprising a nucleic acid sequence encoding one of the aforementioned enzymes, an antisense sequence thereto or a ribozyme therefor, a cell transformed with such a vector, antibodies to the enzymes, a plant cell, a plant tissue, a plant organ or a plant in which the level of an enzyme has been altered, and a method of producing such a plant cell, plant tissue, plant organ or plant. Desirably, alteration of the level of enzyme results in an alteration of the level of acetyl CoA in the plant cell, plant tissue, plant organ or plant. In addition, the present invention provides a recombinant vector comprising an antisense sequence of a nucleic acid sequence ...

PROCESS FOR PREPARING DIPEPTIDYL IV INHIBITORS AND INTERMEDIATES THEREFOR

A process for production of cyclopropyl-fused pyrrolidine-based inhibitors of dipeptidyl peptidase IV is provided which employs a BOC-protected amine of the structure (3) prepared by subjecting an acid of the structure (1) to reduce amination by treating the acid with ammonium formate, nicotinamide adenine dinucleotide, dithiothreitol and partially purified phenylalanine dehydrogenase/formate dehydrogenase enzyme concentrate (PDH/FDH) and without isolating treating the resulting amine of the structure (2) with di-tert-butyl dicarbonate to form the BOC-protected amine.

METHODS FOR THE IDENTIFICATION OF INHIBITORS OF ALPHA-AMINOADIPATE REDUCTASE AND HOMOCITRATE SYNTHASE AS ANTIBIOTICS

The present inventors have discovered that .alpha.-Aminoadipate Reductase and Homocitrate Synthase are each essential for fungal pathogenicity. Specifically, the inhibition of .alpha.-Aminoadipate Reductase or Homocitrate Synthase gene expression in fungi results in no signs of successful infection or lesions. Thus, .alpha.-Aminoadipate Reductase or Homocitrate Synthase can be used as a target for the identification of antibiotics, preferably antifungals. Accordingly, the present invention provides methods for the identification of compounds that inhibit .alpha.-Aminoadipate Reductase or Homocitrate Synthase expression or activity. The methods of the invention are useful for the identification of antibiotics, preferably antifungals.

LINEAR POLYFUNCTIONAL MULTIMER BIOMOLECULE COUPLED TO POLYUBIQUITIN LINKER AND USE THEREOF

The present invention provides a linear multimer biomolecule polymer wherein a biomolecule is bonded to a polyubiquitin scaffold formed of two or more covalently bonded ubiquitins, by obtaining, from a host cell, a biomolecule bonded with a ubiquitin C-terminal tag through recombinant expression, and polyubiquitinating the biomolecule in vitro in the presence of proteins involved in ubiquitination, E1 (activation enzyme), E2 (conjugation enzyme), and E3 (ligase), and a substrate. The polymer according to the present invention may be used in the separation and purification of a biomolecule, the separation of a target material that binds to the biomolecule, etc.

A RECOMBINANT YEAST AND A METHOD FOR PRODUCING ETHANOL USING THE SAME

The invention is intended to metabolize acetic acid in a medium at the time of culture, such as ethanol fermentation by yeast, and to reduce acetic acid concentration. Specifically, the invention relates to a recombinant yeast resulting from introduction of the acetaldehyde dehydrogenase gene (EC 1.2.1.10) and regulation of an enzyme involved with trehalose accumulation.

GENETICALLY ENGINEERED BACTERIUM COMPRISING ENERGY-GENERATING FERMENTATION PATHWAY

MICROBIOLOGICAL PRODUCTION OF 3-HYDROXYISOBUTYRIC ACID

The present invention relates to a cell which has been genetically modifi ed by comparison with its wild type in such a way that it is able to form mo re, by comparison with its wild type, 3-hydroxyisobutyric acid or polyhydrox yalkanoates based on 3-hydroxyisobutyric acid via methylmalonate semialdehyd e or 3-hydroxybutyryl-coenzyme A as precursors. The invention also relates t o a method for producing a genetically modified cell, to the genetically mod ified cell obtainable by this method, to a method for producing 3-hydroxyiso butyric acid or polyhydroxyalkanoates based on 3-hydroxyisobutyric acid, to a method for producing methacrylic acid or methacrylic esters, and to a meth od for producing polymethacrylic acid or polymethacrylic esters. The present invention further relates to an isolated DNA, to a vector, to the use of th is vector for transforming a cell, to a transformed cell, and to a polypepti de.

RECOMBINANT CELL, AND METHOD FOR PRODUCING ISOPRENE

The purpose of the present invention is to provide a series of technologies capable of producing isoprene from a synthesis gas, etc. Provided is a recombinant cell capable of producing isoprene from at least one C1 compound, wherein: a nucleic acid that codes an isoprene synthase has been introduced to a host cell having the ability to synthesize isopentenyl diphosphate by using a non-mevalonate pathway; the nucleic acid is expressed inside the host cell; and said C1 compound is selected from a group comprising carbon monoxide, carbon dioxide, formic acid, and methanol. The host cell is exemplified by a Clostridium cell or a Moorella cell. Also provided is a production method for isoprene using this recombinant cell.

METHODS OF PRODUCING OMEGA-HYDROXYLATED FATTY ACID DERIVATIVES

The disclosure relates to omega-hydroxylated fatty acid derivatives and methods of producing them. Herein, the disclosure encompasses a novel and environmentally friendly production method that provides omega-hydroxylated fatty acid derivatives at high purity and yield. Further encompassed are recombinant microorganisms that produce omega-hydroxylated fatty acid derivatives through selective fermentation.

DEHYDROGENASE-CATALYSED PRODUCTION OF FDCA

The invention relates to a cell expressing a polypeptide having 5-hydroxymethy1-2-furancarboxylic acid dehydrogenase activity, as well as to a cell expressing a polypeptide having furanic compound transport capabilities. The invention also relates to a process for the production of 2,5-furan-dicarboxylic acid (FDCA) wherein the cells of the invention are used for oxidation of a furanic precursors of FDCA.

ZYMOMONAS WITH IMPROVED XYLOSE UTILIZATION

Strains of Zymomonas were engineered by introducing a chimeric xylose isomerase gene that contains a mutant promoter of the Z. mobilis glyceraldehyde-3-phosphate dehydrogenase gene. The promoter directs increased expression of xylose isomerase, and when the strain is in addition engineered for expression of xylulokinase, transaldolase and transketolase, improved utilization of xylose is obtained.

ETHANOL PRODUCTION BY MICROORGANISMS

The present disclosure relates to methods and compositions for engineering photo autotrophic organisms to convert carbon dioxide and light into fatty acid esters and other molecules, including biofuels. The molecules are then secreted by the organism into a growth medium.

ENZYMATIC CONVERSION OF GDP-MANNOSE TO GDP-FUCOSE

This invention provides methods for practical enzymatic conversion of GDP- mannose to GDP-fucose. These methods are useful for efficient synthesis of reactants used in the synthesis of fucosylated oligosaccharides.

METHOD FOR PRODUCING POLYBUTYLENE TEREPHTHALATE

The purpose of the present invention is to provide a production method for polybutylene terephthalate (PBT) having good color tones, said method using a biological resource-derived 1, 4-butanediol (BG). This production method for PBT has: a step in which a dicarboxylic acid component and a diol component including a raw material 1, 4-BG having a nitrogen atom content of 0.01-50 ppm by mass are esterized or transesterified; and a polycondensation step in which PBT is obtained from the reaction product. The gamma-butyrolactone content in the raw material 1, 4-BG is 1-100 ppm by mass.

OXIDOREDUCTASES FOR THE STEREOSELECTIVE REDUCTION OF KETO COMPOUNDS

The invention relates to a process for the enantioselective enzymatic reduction of a keto compound to the corresponding chiral hydroxy compound, wherein the keto compound is reduced with an oxidoreductase in the presence of a cofactor, and is characterized in that an oxidoreductase is used which has an amino acid sequence in which (a) at least 70% of the amino acids are identical to the amino acids of one of the amino acid sequences SEQ ID No 1, SEQ ID No 6 and SEQ ID No 8, or (b) at least 55% of the amino acids are identical to the amino acids of the amino acid sequence SEQ ID No 2, or (c) at least 65% of the amino acids are identical to the amino acids of the amino acid sequence SEQ ID No 3, or (d) at least 75% of the amino acids are identical to the amino acids of the amino acid sequence SEQ ID No 4, or (e) at least 65% of the amino acids are identical to the amino acids of the amino acid sequence SEQ ID No 5, or (f) at least 50% of the amino acids are identical to the amino acids of ...

ACYL-ACP REDUCTASE WITH IMPROVED PROPERTIES

The disclosure relates to acyl-ACP reductase (AAR) enzyme variants that result in improved fatty aldehyde and fatty alcohol production when expressed in recombinant host cells. The disclosure further relates to methods of making and using such AAR variants for the production of fatty alcohol compositions having particular characteristics.

GENES ENCODING BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE COMPLEX FROM STREPTOMYCES AVERMITILIS

The present invention relates to novel DNA sequences that encode for the branched-chain alpha-ketoacid dehydrogenase complex of an organism belonging to the genus Streptomyces and to novel polypeptides produced by the expression of such sequences. It also relates to novel methods of enhancing the production of natural avermectin, of producing a Streptomyces avermitilis bkd mutant and of producing novel avermectins through fermentation.

PRODUCTION OF PLANTS RESISTANT TO ATTACKS OF SCLEROTINIA SCLEROTIORUM BY INTRODUCING A GENE CODING FOR AN OXALATE OXIDASE

... 1) DNA sequence encoding an oxalate oxidase. 2) The protein may be used for the resistance of plants to diseases caused by Sclerotinia sp. It may be provided by a chimeric gene and a vector containing the coding sequence. 3) It may be used to confer on plants an increased resistance to diseases caused by Sclerotinia sp.

DNA SEQUENCES CODING FOR A CINNAMOYL COA REDUCTASE, AND APPLICATIONS THEREOF IN THE CONTROL OF LIGNIN CONTENTS IN PLANTS

La présente invention concerne tout séquence d'ADN comprenant à titre de région codante, tout ou partie de la séquence nucléotidique codant pour un ARNm codant pour une cinnamoyl CoA réductase (CCR) chez la luzern e et/ou le maïs, ou tout ou partie de la séquence nucléotidique complémentaire de ces dernières et codant pour un ARNm antisens su sceptible de s'hybrider avec l'ARNm susmentionné. L'invention vise également l'utilisation des séquences susmentionnées pour la mi se en oeuvre de procédés de régulation de la biosynthèse de lingnines chez les plantes.

GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AND NUCLEAR RESTORATION OF CYTOPLASMIC MALE STERILITY

The present invention relates to a marker for nuclear restoration of cytoplasmic male sterility, and more particularly to the use of glyceraldehyde-3-phosphate dehydrogenase complementary DNA as such a marker. There is provided a gene for nuclear restoration of cytoplamic male sterility, and more particularly to the use of a form of the gene encoding glyceraldehyde-3-phosphate dehydrogenase for this purpose. Finally, there is provided a method for the production of restorer lines directly through genetic transformation of plants with such a gene.

IMPROVED METHODS FOR TRANSFORMING PHAFFIA STRAINS, TRANSFORMED PHAFFIA STRAINS SO OBTAINED AND RECOMBINANT DNA IN SAID METHODS

The present invention provides recombinant DNA comprising a transcription promoter and a downstream sequence to be expressed, in operable linkage therewith, wherein the transcription promoter comprises a region found upstream of the open reading frame of a highly expressed Phaffia gene, preferably a glycolytic pathway gene, more preferably the gene coding for Glyceraldehyde-3-Phosphate Dehydrogenase. Further preferred recombinant DNAs according to the invention contain promoters of ribosomal protein encoding genes, more preferably wherein the transcription promoter comprises a region found upstream of the open reading frame encoding a protein as represented by one of the amino acid sequences depicted in any one of SEQIDNOs: 24 to 50. According to a further aspect of the invention an isolated DNA sequence coding for an enzyme involved in the carotenoid biosynthetic pathway of Phaffia rhodozyma is provided, preferably wherein said enzyme has an activity selected from isopentenyl pyrophosphate ...

PROCESS FOR THE PREPARATION OF PANTOTHENIC ACID BY AMPLIFICATION OF NUCLEOTIDE SEQUENCES WHICH CODE FOR KETOPANTOATE REDUCTASE

The invention relates to a process for the preparation and improvement of D-pantothenic acid-producing microorganisms by amplification of nucleotide sequences which code for ketopantoate reductase, in particular the panE gene, individually or in combination with one another, and optionally additionally of the ilvC gene, the microorganisms containing these nucleotide sequences, and a process for the preparation of D-pantothenic acid comprising fermentation of these microorganisms, concentration of pantothenic acid in the medium or in the cells of the microorganisms, and isolation of the D-pantothenic acid.

PROCEDURE FOR THE REGULATION BY FORMATE OR FOR THIS REAGENT SUITABLE IN FORMATE TRANSFER-CASH CONNECTIONS AND.

PROCEDURE FOR THE ISOLATION AND PURE REPRESENTATION OF ENZYMES AND ADSORBENT FOR THE EXECUTION OF THE PROCEDURE.

POLYPEPTIDES WITH OXIDOREDUCTASE ACTIVITY AND THEIR USE

GENETICALLY CONSTRUCTED BACTERIUM, CONTAINING ENERGOGENERIRUYuShchII ENZYMATIC PATH

STRAINS OF YEAST, CONSTRUCTED FOR PRODUCING ETHANOL FROM ACETIC ACID AND GLYCEROL

Preparation of adipic acid

The invention relates to a method for preparing adipic acid, comprising converting alpha-ketoglutaric acid (AKG) into alpha-ketoadipic acid (AKA), converting alpha-ketoadipic acid into alpha-ketopimelic acid (AKP), converting alpha-ketopimelic acid into 5-formylpentanoic acid (5-FVA), and converting 5-formylpentanoic acid into adipic acid, wherein at least one of these conversions is carried out using a heterologous biocatalyst.The invention further relates to a heterologous cell, comprising one or more heterologous nucleic acid sequences encoding one or more heterologous enzymes capable of catalysing at least one reaction step in said method.

Yeast organism producing isobutanol at a high yield

The present invention provides recombinant microorganisms comprising an isobutanol producing metabolic pathway and methods of using said recombinant microorganisms to produce isobutanol. In various aspects of the invention, the recombinant microorganisms may comprise a modification resulting in the reduction of pyruvate decarboxylase and/or glycerol-3-phosphate dehydrogenase activity. In various embodiments described herein, the recombinant microorganisms may be microorganisms of the Saccharomyces clade, Crabtree-negative yeast microorganisms, Crabtree-positive yeast microorganisms, post-WGD (whole genome duplication) yeast microorganisms, pre-WGD (whole genome duplication) yeast microorganisms, and non-fermenting yeast microorganisms.

Method for tracing gram-negative bacteria inside animal model using stable and bioluminescence-based expression system therefor

A method of creating a biotechnological product and an efficient and stable bio-luminescence vector which could be used for tracking Gram-negative bacteria when distributing inside animal body are provided. Through conjugation, this auto-luminescence vector can be easily transmitted from bacteria to bacteria among Gram-negative bacteria, and may facilitate bacteria to be luminescence-labeled for subsequently analyzing the dynamic change of bio-luminescent bacteria within animal body in vivo. This system includes a lacZ promoter-driven luxABCDE, a high copy number of ColE1 replicon, and a high plasmid stability of the conjugative and broad host-ranged plasmid pSE34 from Salmonella enterica serovar Enteritidis Sal550. This resulting construct pSE-Lux1 can not only conjugatively transmit among bacteria with broad host range, but also stably maintain in bacteria to efficiently express the bio-luminescent luxABCDE without supplementing the subtract for luciferases and the antibiotics for plasmid selection.

Lipid Production

The present invention relates to a genetically modified Acinetobacter host for lipid production. The Acinetobacter host has been genetically modified to be deficient of one or more of genes A) a gene encoding fatty acyl-CoA reductase (EC1.2.1.n2), wherein said host is capable of increased production of TAGs and/or of total lipids compared to the parent host; and/or B) a gene encoding lipase (EC:3.1.1.3), a gene encoding pyruvate dehydrogenase (EC:1.2.2.2), and/or gene ACIAD 2177, or functional equivalents of any of said genes, wherein said host is capable of increased production of wax esters and/or total lipids compared to the parent host.

Preparation of alpha-ketopimelic acid

The invention relates to a method for preparing alpha-ketopimelic acid, comprising converting alpha-ketoglutaric acid into alpha-ketoadipic acid and converting alpha-ketoadipic acid into alpha-ketopimelic acid, wherein at least one of these conversions is carried out using a heterologous biocatalyst. The invention further relates to a heterologous cell, comprising one or more heterologous nucleic acid sequences encoding one or more heterologous enzymes capable of catalysing at least one reaction step in the preparation of alpha-ketopimelic acid from alpha-ketoglutaric acid.

Renewable chemicals and fuels from oleaginous yeast

The invention provides methods of cultivating oil-bearing microbes using xylose alone or in combination with other depolymerized cellulosic material. Also provided are microorganisms comprising an exogenous gene encoding a polysaccharide degrading enzyme, such as a cellulase, a hemicellulase, a pectinase, or a driselase. Some methods of microbial fermentation are provided that comprise the use of xylose and depolymerized cellulosic materials for the production of oil-bearing microorgansims.

Reductase Enzymes

In some embodiments, the present invention relates to isolated enzymes useful in reducing a fatty acyl-CoA to a corresponding fatty alcohol in a single biosynthetic step, polynucleotides encoding the enzymes, and methods for making and using these polynucleotides and enzymes. In some embodiments, the invention provides for isolated or recombinant enzymes capable of reducing a fatty acyl-CoA to a fatty alcohol. In still another embodiment, the invention provides for isolated or recombinant polynucleotides encoding an enzyme capable of reducing a fatty acyl-CoA to a fatty alcohol. In other embodiments, the invention provides for methods of making or using enzymes capable of reducing fatty acyl-CoA to a fatty alcohol, and methods of making using polynucleotides that encode the enzymes.

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

The present invention comprises methods and compositions for the reduction of oxalate in humans, and methods for the purification and isolation of recombinant oxalate reducing enzyme proteins. The invention provides methods and compositions for the delivery of oxalate-reducing enzymes in particle compositions. The compositions of the present invention are suitable in methods of treatment or prevention of oxalate-related conditions.

Production of fatty alcohols with fatty alcohol forming acyl-coa reductases (far)

The disclosure relates to methods of producing fatty alcohols from recombinant host cells comprising genes encoding heterologous fatty acyl-CoA reductase (FAR) enzymes. The disclosure further relates to FAR enzymes and functional fragments thereof derived from marine bacterium and particularly marine gamma proteobacterium such as Marinobacter and Oceanobacter ; polynucleotides encoding the FAR enzymes and vectors and host cells comprising the same.

Cell-free preparation of carbapenems

Provided herein are cell-free systems for generating carbapenems, e.g., a compound of the Formula (I): or salts thereof; wherein , R 1 , R 2 , R 3 , R 4 , R 5 , and R 6 are defined herein. Also provided are pharmaceutical compositions comprising a compound generated by the inventive cell-free system, and use of these compounds and compositions for the treatment of bacterial infections.

Native nad-dependent gapdh replaced with nadp-dependent gapdh plus nadk

This invention is metabolically engineer bacterial strains that provide increased intracellular NADPH availability for the purpose of increasing the yield and productivity of NADPH-dependent compounds. In the invention, native NAD-dependent GAPDH is replaced with NADP-dependent GAPDH plus overexpressed NADK. Uses for the bacteria are also provided.

Industrial fatty acid engineering general system for modifying fatty acids

Compositions and methods for a hybrid biological and chemical process utilizing chemotrophic microorganisms that converts syngas and/or gaseous CO2 and/or a mixture of CO2 gas and H2 gas into one or more desaturated hydrocarbons, unsaturated fatty acids, hydroxy acids, or diacids.

Novel expression-regulating sequences and expression products in the field of filamentous fungi

The invention pertains to novel proteins corresponding to Chrysosporium glycosyl hydrolases of families 7 and 10, exhibiting a minimum aminoacid identity of 70 and 75%, respectively, with the amino acid sequence of SEQ ID No's 2 and 4, and to a protein corresponding to a Chrysosporium glyceraldehyde phosphate dehydrogenase, exhibiting at least 86% amino acid identity with the partial amino acid sequence of SEQ ID No. 6. The invention further relates to nucleic acid sequences encoding these proteins, and especially to promoter sequences regulating the expression of the corresponding genes. The preferred host for expressing these genes is a fungus, especially a Chrysosporium strain.

Fermentive production of four carbon alcohols

Methods for the fermentative production of four carbon alcohols is provided. Specifically, butanol, preferably isobutanol is produced by the fermentative growth of a recombinant bacterium expressing an isobutanol biosynthetic pathway.

Methods, Systems And Compositions Related To Reduction Of Conversions Of Microbially Produced 3-Hydroxyproplonic Acid (3-HP) To Aldehyde Metabolites

The present invention relates to methods, systems and compositions, including genetically modified microorganisms, directed to achieve decreased microbial conversion of 3-hydroxypropionic acid (3-HP) to aldehydes of 3-HP. In various embodiments this is achieved by disruption of particular aldehyde dehydrogenase genes, including multiple gene deletions. Among the specific nucleic acids that are deleted whereby the desired decreased conversion is achieved are aldA, aldB, puuC), and usg of E. coli. Genetically modified microorganisms so modified are adapted to produce 3-HP, such as by approaches described herein.

NOVEL OXIDOREDUCTASES FOR ENANTIOSELECTIVE REACTIONS

Described herein are compositions and methods for generating oxidoreductases for enantioselective reactions. Described herein are compositions and methods for generating neomorphic (R)-2-hydroxyacid dehydrogenases capable of enzymatically converting a 1-carboxy-2-ketoacid to a 1-carboxy-(R)-2-hydroxyacid, or the reverse reaction. Illustrative examples include (a) (R)-2-hydroxyadipate dehydrogenase and uses thereof for converting 2-oxoadipate to (R)-2-hydroxyadipate, or the reverse reaction; and (b) (R)-2-hydroxyglutarate dehydrogenase and uses thereof for converting 2-oxoglutarate to (R)-2-hydroxyglutarate, or the reverse reaction. Also described herein are compositions and methods for generating non-natural microbial organisms to enzymatically convert 2-oxoadipate to (E)-2-hexenedioate or adipate, or to enzymatically convert 2-oxoglutarate to (E)-2-pentenedioate or glutarate, or the respective reverse reactions. 197-. (canceled)98. A polynucleotide comprising a nucleotide sequence encoding a polypeptide comprising a functional (R)-2-hydroxyacid dehydrogenase useful for catalyzing the enantioselective conversion of a 1-carboxy-2-ketoacid to a 1-carboxy-(R)-2-hydroxyacid , or the reverse reaction , wherein the encoded polypeptide is any one of SEQ ID NOs: 4 , 6 , 8 , 10 , 12 , 14 , 16 , 18 , 22 , 26 , 30 , 34 , or 35-138 , or a degenerate or homologous variant thereof.99. The polynucleotide of claim 98 , wherein the encoded polypeptide is at least 90% identical to the polypeptide sequences shown in SEQ ID NOs: 2 claim 98 , 4 claim 98 , 6 claim 98 , 8 claim 98 , 10 claim 98 , 12 claim 98 , 14 claim 98 , 16 claim 98 , 18 claim 98 , 20 claim 98 , 22 claim 98 , 24 claim 98 , 26 claim 98 , 28 claim 98 , 30 claim 98 , 32 claim 98 , 34 claim 98 , or 35-153;with the proviso that the encoded polypeptide has at least one or more mutations to the active site at positions analogous to V111, R114, R115, R124, R143, or Y150 of SEQ ID NO: 2;wherein the one or more mutations disrupt ...

Recombinant microorganisms and uses therefor

Bacteria are genetically engineered to produce 3-hydroxypropionate (3-HP). The bacteria are carboxydotrophic acetogens. The bacteria produce acetyl-coA using the Wood-Ljungdahl pathway for fixing CO/CO 2 . A malonyl-coA reductase from a bacterium that contains such an enzyme is introduced. Additionally, an acetyl-coA carboxylase may also be introduced The production of 3-HP can be improved by overproduction of acetyl-CoA carboxylase or by overproduction of biotin. This can be effected by improved promoters or higher copy number or enzymes that are catalytically more efficient.

COMPOSITIONS AND METHODS FOR MODULATING AMPA RECEPTOR-MEDIATED EXCITOTOXICITY

The present invention provides AMPAR excitotoxicity mediating polypeptides comprising the GAPDH(2-2-1-1) (I221-E250)amino acid sequence (SEQ ID NO:2). Also disclosed are nucleotide sequences encoding the polypeptides, methods of inhibiting GAPDH association with the GluR2 subunit or p53. Methods of inhibiting AMPA receptor mediated excitotoxicity using the polypeptides and nucleic acids are also disclosed. 1. An excitotoxicity-inhibiting polypeptide comprising an amino acid sequence that modulates Glu-R2-containing AMPA receptor signal transduction , wherein said polypeptide does not encompass a naturally occurring GAPDH polypeptide.2. The excitotoxicity-inhibiting polypeptide of claim 1 , comprising a GAPDH(2-2-1-1) (I221-E250) amino acid sequence (SEQ ID NO:2) claim 1 , or a sequence which is at least 80% identical to SEQ ID NO:2 that binds to p53 and wherein said polypeptide does not encompass a naturally occurring full length GAPDH polypeptide.3. The polypeptide of claim 2 , wherein said polypeptide is a fusion protein.4. The polypeptide of claim 3 , wherein said fusion protein comprises a protein transduction domain.5. The polypeptide of claim 2 , said polypeptide is attached covalently or non-covalently to a non-protein substrate claim 2 , non-protein molecule claim 2 , non-protein macromolecule claim 2 , a support claim 2 , or any combination thereof.6. The polypeptide of claim 5 , wherein the polypeptide claim 5 , non-protein substrate claim 5 , non-protein molecule claim 5 , non-protein macromolecule claim 5 , support or any combination thereof is labeled.7. A nucleic acid encoding the polypeptide of .8. A method of inhibiting AMPA receptor-mediated excitotoxicity comprising claim 2 , administering claim 2 ,a polypeptide comprising the GAPDH(2-2-1-1) (I221-E250) amino acid sequence (SEQ ID NO:2)ora nucleic acid capable of expressing a polypeptide comprising the GAPDH(2-2-1-1) (I221-E250) amino acid sequence (SEQ ID NO:2), to a cell, tissue or subject in ...

IMPROVED PRODUCTION OF ANTI-PEPTIDE ANTIBODIES

Anti-peptide antibodies (APAs) are extremely important tools for biomedical research. Many important techniques, such as immunoblots, ELISA immunoassays, immunocytochemistry, and protein microarrays are intrinsically linked to APA function and completely dependent on APA quality. Unfortunately, not all commercially-available APAs have good antigen binding characteristics; as a result, researchers are often unable to perform high quality protein analysis experiments. This disclosure describes a new method for the scalable production of polyclonal APAs using recombinant antigens. These recombinant peptide antigens have several advantages over traditional peptide antigens which improve the ease and speed of antibody production. The recombinant antigens can be scalably produced and purified much faster than traditional synthetic peptide-conjugates. These recombinant antigen-carriers are designed to specifically aggregate in vivo after administration into the host; this aggregation greatly enhances immunogenicity and may eliminate the need for the use of chemical adjuvants which cause physical irritation and discomfort to the host. 127-. (canceled)28. A compound comprising a peptide antigen fused to a carrier protein , wherein the carrier protein comprises a thermally-responsive polypeptide sequence capable of causing the compound to aggregate when heated to temperatures above about 30° C.29. The compound of claim 28 , wherein the peptide antigen has a length of up to about 40 amino acids.30. The compound of claim 28 , wherein the carrier protein is GroEL protein fused to a thermally-responsive aggregation polypeptide sequence31. The compound of claim 28 , wherein the carrier protein is GAPDH protein fused to a thermally-responsive aggregation polypeptide sequence32E. coli. The compound of claim 28 , wherein the carrier protein comprises an acceptor sequence which is heptosylated when expressed in an strain expressing the aah (bacterial heptosyl-transferase) enzyme or ...

Fermentive Production of Four Carbon Alcohols

Methods for the fermentative production of four carbon alcohols is provided. Specifically, butanol, preferably isobutanol is produced by the fermentative growth of a recombinant bacterium expressing an isobutanol biosynthetic pathway.

Fatty alcohol forming acyl reductases (fars) and methods of use thereof

The present disclosure provides methods useful for producing fatty alcohol compositions from recombinant host cells. The disclosure further provides variant fatty acyl-CoA reductase (FAR) enzymes, polynucleotides encoding the variant FAR enzymes, and vectors and host cells comprising the same.

XYLR Mutant For Improved Xylose Utilization Or Improved Co-Utilization Of Glucose And Xylose

The disclosure relates to mutant gene(s) that confer upon microorganisms that express them an improved capacity to utilize xylose and improved capacity to co-utilize glucose and xylose thereby resulting in improved growth of the microorganism. Further encompassed are methods of producing fatty acids and fatty acid derivatives from cellulosic biomass, xylose, and/or a glucose/xylose mix by employing the host cells expressing the engineered XylR variants and compositions of biologically produced fatty acids and fatty acid derivatives. 1. A XylR protein variant , wherein the XylR protein variant has at least one mutation at a position selected from positions 83 , 88 , 89 , 112 , 120 , 141 , 145 , 146 , 147 , 150 , 154 , 155 , 247 , 270 , 280 , 286 , 289 , 295 , 305 , 306 , 313 , 333 , 336 , 337 , 351 , 364 , 365 , 372 , and 382 of SEQ ID NO: 1.2. A recombinant host cell comprising the XylR protein variant of .3. A method for increasing xylose utilization in a recombinant host cell claim 2 , the method comprising culturing in a culture medium comprising xylose claim 2 , the recombinant host cell of claim 2 , wherein expression of the XylR protein variant confers improved xylose utilization of the recombinant host cell in comparison to the xylose utilization of a host cell expressing SEQ ID NO: 1 when the cells are cultured in the presence of xylose.4. The method of claim 3 , wherein the method is used for preparing a fatty acid derivative claim 3 , the method comprising culturing in a culture medium comprising xylose claim 3 , a recombinant host cell which further comprises at least one heterologous fatty acid derivative biosynthetic enzyme.5. The method of claim 4 , wherein the fatty acid derivative is: a fatty acid ester and wherein at least one heterologous fatty acid derivative biosynthetic enzyme has ester synthase activity claim 4 , and optionally wherein at least one heterologous fatty acid derivative biosynthetic enzyme is a thioesterase; a ω-hydroxy fatty acid ...

Construction and Application of Engineered Strain of Escherichia Coli for Producing Malic Acid by Fixing CO2

The disclosure discloses construction and application of an engineered strain of E. coli for producing malic acid by fixing CO2, and belongs to the field of fermentation. The engineered strain is obtained by performing genetic engineering transformation on Escherichia coli MG1655; the genetic engineering transformation includes knocking out a fumarate reductase gene, a fumarase gene, a lactate dehydrogenase gene and an alcohol dehydrogenase gene and freely overexpressing a formate dehydrogenase, an acetyl coenzyme A synthetase, an acylated acetaldehyde dehydrogenase, a formaldehyde lyase, a dihydroxyacetone kinase, a malic enzyme and a phosphite oxidoreductase to obtain a strain GH0407. The strain is used for producing malic acid by fermentation, anaerobic fermentation is performed for 72 hours with CO2 and glucose as a co-substrate, the production of malic acid reaches 39 g/L, the yield is 1.53 mol/mol, and accumulation of malic acid in the original strain is not achieved.

Method for producing ethanol using recombinant yeast

The invention is intended to metabolize acetic acid and to lower acetic acid concentration in a medium at the time of xylose assimilation and ethanol fermentation by a yeast strain having xylose-metabolizing ability. The method for producing ethanol comprises a step of culturing recombinant yeast strains resulting from introduction of a xylose isomerase gene and an acetaldehyde dehydrogenase gene into a medium containing xylose, so as to perform ethanol fermentation.

MICROORGANISMS HAVING PUTRESCINE PRODUCTIVITY AND PROCESS FOR PRODUCING PUTRESCINE USING THE SAME

The present invention relates to a recombinant microorganism capable of producing putrescine, in which the microorganism is modified to have enhanced NCgl2522 activity, thereby producing putrescine in a high yield, and a method for producing putrescine using the microorganism. 1. A microorganism having putrescine productivity , which is modified to have enhanced activity of a protein having an amino acid sequence represented by SEQ ID NO: 21 or 23.2. The microorganism having putrescine productivity according to claim 1 , wherein the microorganism is further modified to have weakened activities of ornithine carbamoyltransferase (ArgF) and a protein (NCgl1221) involved in glutamate export claim 1 , compared to the endogenous activities claim 1 , and to have enhanced ornithine decarboxylase (ODC) activity.3. The microorganism having putrescine productivity according to claim 2 , wherein the ornithine carbamoyltransferase (ArgF) has an amino acid sequence represented by SEQ ID NO: 29 claim 2 , the protein (NCgl1221) involved in glutamate export has an amino acid sequence represented by SEQ ID NO: 30 claim 2 , and the ornithine decarboxylase (ODC) has an amino acid sequence represented by SEQ ID NO: 33.4. The microorganism having putrescine productivity according to claim 1 , wherein the microorganism is further modified to have enhanced activities of acetyl-gamma-glutamyl-phosphate reductase (ArgC) claim 1 , acetylglutamate synthase or ornithine acetyltransferase (ArgJ) claim 1 , acetylglutamate kinase (ArgB) claim 1 , and acetylornithine aminotransferase (ArgD) claim 1 , compared to the endogenous activities.5. The microorganism having putrescine productivity according to claim 4 , wherein the acetyl-gamma-glutamyl-phosphate reductase (ArgC) claim 4 , acetylglutamate synthase or ornithine acetyltransferase (ArgJ) claim 4 , acetyl glutamate kinase (ArgB) claim 4 , and acetylornithine aminotransferase (ArgD) have amino acid sequences represented by SEQ ID NOs: 25 claim 4 ...

Synthetic carbon fixation pathways

The present disclosure relates to methods for more efficiently recycling reduced electron carriers in a hydrogen-oxidizing microorganism with an operable Calvin-Benson cycle; synthetic carbon fixation pathways that recycle reduced electron carriers more efficiently than the Calvin-Benson cycle, such as methods for enzymatically converting carbon dioxide to formate and assimilating the resulting formate into central carbon metabolism; methods for producing biochemical products; and recombinant hosts utilizing one or more synthetic carbon fixation pathways.

Methods, reagents and cells for biosynthesizing compounds

This document describes biochemical pathways for producing 7-hydroxyheptanoate methyl ester and heptanoic acid heptyl ester using one or more of a fatty acid O-methyltransferase, an alcohol O-acetyltransferase, and a monooxygenase, as well as recombinant hosts expressing one or more of such exogenous enzymes. 7-hydroxyheptanoate methyl esters and heptanoic acid heptyl esters can be enzymatically converted to pimelic acid, 7-aminoheptanoate, 7-hydroxyheptanoate, heptamethylenediamine, or 1,7-heptanediol.

METABOLIC ENGINEERING FOR MICROBIAL PRODUCTION OF TERPENOID PRODUCTS

The invention relates to methods and bacterial strains for making terpene and terpenoid products, the bacterial strains having improved carbon pull through the MEP pathway and to a downstream recombinant synthesis pathway. 1. A method for production of a terpene or terpenoid product , comprising:providing a bacterial strain that produces isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) through an upstream methylerythritol phosphate pathway (MEP pathway) and converts the IPP and DMAPP to a terpene or terpenoid product through a downstream synthesis pathway;wherein IspG and IspH are overexpressed in the bacterial strain such that IspG activity and IspH activity are balanced to provide increased carbon flux to 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) intermediate, while preventing accumulation of HMBPP at an amount that feeds back and reduces MEP pathway flux and terpene or terpenoid productivity, the strain optionally comprising one or more genetic modifications that enhance supply and/or transfer of electrons through the MEP pathway and/or to terpene and terpenoid products, and culturing the bacterial strain to produce the terpene or terpenoid product.2EscherichiaBacillusCorynebacteriumRhodobacterZymomonasVibrioPseudomonas. The method of claim 1 , wherein the bacterial strain is a bacteria selected from spp. claim 1 , spp. claim 1 , spp. claim 1 , spp. claim 1 , spp. claim 1 , spp. claim 1 , and spp.3Escherichia coli, Bacillus subtilis, Corynebacterium glutamicum, Rhodobacter capsulatus, Rhodobacter sphaeroides, Zvmomonas mobilis, Vibrio natriegensPseudomonas putida.. The method of claim 2 , wherein the bacterial strain is a species selected from claim 2 , or4E. coli.. The method of claim 3 , wherein the bacterial strain is5. The method of any one of to claim 3 , wherein the bacterial strain expresses dxs claim 3 , ispD claim 3 , ispF claim 3 , and idi as recombinant genes claim 3 , which are optionally expressed as an operon.6. The ...

PUTRESCINE-PRODUCING MICROORGANISM AND METHOD FOR PRODUCING PUTRESCINE USING THE SAME

The present application relates to a putrescine-producing microorganism in which the activity of formate dehydrogenase is increased, and a method for producing putrescine using the same. 1Corynebacterium. A putrescine-producing microorganism of the genus , in which the activity of formate dehydrogenase (Fdh) is increased compared to that before modification.2Candida boidinii.. The microorganism according to claim 1 , wherein the Fdh is derived from3. The microorganism according to claim 1 , wherein the Fdh consists of the amino acid sequence of SEQ ID NO: 10.4. The microorganism according to claim 1 , wherein the activity of ornithine decarboxylase (ODC) is further introduced.5. The microorganism according to claim 1 , wherein the activity of acetyltransferase is further weakened compared to its endogenous activity.6. The microorganism according to claim 1 , wherein the activity of the protein that exhibits the activity of exporting putrescine is increased compared to its endogenous activity.7Corynebacterium glutamicum.. The microorganism according to claim 1 , wherein the microorganism is8. A method of producing putrescine claim 1 , comprising:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, '(a) culturing the microorganism of in a medium; and'}(b) recovering putrescine from the microorganism or the cultured medium obtained in step (a).9. The method according to claim 8 , wherein the microorganism is cultured in a medium not containing formic acid.10. The method according to claim 8 , wherein the microorganism is cultured under an aerobic condition.11. A method of producing putrescine claim 2 , comprising: (a) culturing the microorganism of in a medium; and (b) recovering putrescine from the microorganism or the cultured medium obtained in step (a).12. A method of producing putrescine claim 3 , comprising: (a) culturing the microorganism of in a medium; and (b) recovering putrescine from the microorganism or the cultured medium obtained in step (a).13. A method of ...

Metabolic engineering for microbial production of terpenoid products

The invention relates to methods and bacterial strains for making terpene and terpenoid products, the bacterial strains having improved carbon pull through the MEP pathway and to a downstream recombinant synthesis pathway.

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 ...

MICROORGANISM HAVING NOVEL ACRYLIC ACID SYNTHESIS PATHWAY HAVING ENHANCED ACTIVITY OF COA ACYLATING ALDEHYDE DEHYDROGENASE AND METHOD OF PRODUCING ACRYLIC ACID USING THE SAME

A microorganism capable of producing acrylic acid, comprising a genetic modification that increases activity of CoA acylating aldehyde dehydrogenase (ALDH) catalyzing conversion of 3-hydroxypropionaldehyde (3-HPA) to 3-hydroxy propionyl-CoA (3-HP-CoA) and a genetic modification that increases activity of 3-HP-CoA dehydratase catalyzing conversion of 3-HP-CoA to acrylyl-CoA in the microorganism in comparison with a cell that is not genetically engineered; as well as a method of producing the microorganism, and a method of producing acrylic acid using the same. 1. A genetically engineered microorganism that produces acrylate , wherein the genetically engineered microorganism comprisesa genetic modification that increases CoA acylating aldehyde dehydrogenase (ALDH) activity in catalyzing conversion of 3-hydroxypropionaldehyde (3-HPA) to 3-hydroxy propionyl-CoA (3-HP-CoA); anda genetic modification that increases 3-HP-CoA dehydratase activity in catalyzing conversion of 3-HP-CoA to acrylyl-CoA;in comparison with a microorganism of the same type that is not genetically engineered.2. The microorganism of claim 1 , further comprises a genetic modification that increases activity of an enzyme that catalyzes conversion of acrylyl-CoA to acrylate in comparison with a microorganism of the same type that is not genetically engineered.3. The microorganism of claim 1 , wherein the ALDH has an amino acid sequence comprising one of SEQ ID NOs: 1 to 20.4. The microorganism of claim 1 , wherein the ALDH belongs to EC 1.2.1.10 claim 1 , or EC 1.2.1.87.5. The microorganism of claim 1 , wherein the ALDH is propionaldehyde dehydrogenase (pduP).6. The microorganism of claim 1 , wherein the 3-HP-CoA dehydratase has an amino acid sequence comprising one of SEQ ID NOs: 41 to 119.7. The microorganism of claim 1 , wherein the 3-HP-CoA dehydratase belongs to EC 4.2.1.8. The microorganism of claim 2 , wherein the enzyme that catalyzes conversion of acrylyl-CoA to acrylate has an amino acid ...

MICROBIAL PRODUCTION OF N-BUTYRALDEHYDE

Microorganisms and methods of producing n-butyraldehyde with enhanced yields are presented in which a microorganism is engineered to enhance the conversion of a carbon source into n-butyraldehyde. The n-butyraldehyde is recovered by way of a gas stripping process that occurs during the conversion process, providing significantly greater product yield than post-fermentation recovery of n-butyraldehyde alone. 2. The microorganism of claim 1 , wherein the acetyl-CoA acetyltransferase has an E.C. number of 2.3.1.9.3. The microorganism of claim 1 , wherein the 3-hydroxyacyl-CoA dehydrogenase has an E.C. number of 1.1.1.157.4. The microorganism of claim 1 , wherein the crotonyl-CoA hydratase has an E.C. number of 4.2.1.55.5. The microorganism of claim 1 , wherein the butyryl-CoA dehydrogenase has an E.C. number of 1.3.99.2.6. The microorganism of claim 1 , wherein the trans-enoyl-CoA reductase has an E.C. number of 1.3.1.38.7. The microorganism of claim 1 , wherein the butanal dehydrogenase has an E.C. number of 1.2.1.57.8. The microorganism of claim 1 , wherein the at least one native gene is selected from the group consisting of ldhA claim 1 , adhE claim 1 , frdBC claim 1 , pta claim 1 , and yqhD.9. The microorganism of claim 1 , wherein the at least one native gene are ldhA claim 1 , adhE claim 1 , and frdBC.10. The microorganism of claim 1 , wherein the at least one native gene are ldhA claim 1 , adhE claim 1 , frdBC claim 1 , pta claim 1 , and yqhD.11. The microorganism of claim 1 , wherein at least one native gene is deleted to reduce alcohol production by at least 70%.12. The microorganism of claim 1 , wherein at least one native gene is deleted to reduce alcohol production by at least 90%.13. The microorganism of claim 1 , wherein the genetically modified microorganism produces a cumulative yield of 2.0 g/L n-butyraldehyde at or before 40 hours of culture time.14. The microorganism of claim 1 , wherein the genetically modified microorganism produces 50% of a ...

ACYL-ACP REDUCTASE WITH IMPROVED PROPERTIES

The disclosure relates to acyl-ACP reductase (AAR) enzyme variants that result in improved fatty aldehyde and fatty alcohol production when expressed in recombinant host cells. The disclosure further relates to methods of making and using such AAR variants for the production of fatty alcohol compositions having particular characteristics. 182.-. (canceled)83. A variant acyl-ACP reductase (AAR) polypeptide comprising at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 80 , wherein said variant AAR polypeptide comprises a mutation at amino acid position selected from the group consisting of Q40V , G52V , G273E , K303G , H340P , L344A , L344D , L344S , L344T , A345R , V346P , V346G , and A345* , and wherein said AAR polypeptide catalyzes the conversion of an acyl-ACP to a fatty aldehyde.84. The variant AAR polypeptide of claim 83 , wherein expression of the variant AAR polypeptide in a recombinant host cell results in a higher titer of a fatty aldehyde or fatty alcohol composition as compared to a titer of a fatty aldehyde or fatty alcohol composition produced by expression of a wild type AAR polypeptide in a corresponding wild type host cell.85. The variant AAR polypeptide of claim 83 , wherein said fatty alcohol composition is a C12 claim 83 , C14 or C16 fatty alcohol composition claim 83 , or a combination thereof.86. A recombinant host cell expressing the variant AAR polypeptide of .87. The recombinant host cell of claim 86 , wherein the recombinant host cell produces a fatty aldehyde or fatty alcohol composition with a titer that is at least 10% greater claim 86 , at least 15% greater claim 86 , at least 20% greater claim 86 , at least 25% greater claim 86 , or at least 30% greater than the titer of a fatty aldehyde or alcohol composition produced by a host cell expressing a corresponding wild type AAR polypeptide claim 86 , when cultured in medium containing a carbon source under conditions effective to express the variant AAR polypeptide.88. ...

METHOD FOR THE PRODUCTION OF ISOAMYL ALCOHOL

Described is a method for the production isoamyl alcohol (3-methylbutan-1-ol) comprising the enzymatic conversion of 3-methylbutyryl-CoA (isovaleryl-CoA) into isoamyl alcohol comprising: (a) two enzymatic steps comprising (i) first the enzymatic conversion of 3-methylbutyryl-CoA into 3-methylbutyraldehyde (3-methylbutanal or isovaleraldehyde); and (ii) then enzymatically converting the thus obtained 3-methylbutyraldehyde into said isoamyl alcohol; or (b) a single enzymatic reaction in which 3-methylbutyryl-CoA is directly converted into isoamyl alcohol by making use of an alcohol-forming short chain acyl-CoA dehydrogenase/fatty acyl-CoA reductase or an alcohol-forming fatty acyl-CoA reductase (long-chain acyl-CoA:NADPH reductase) (EC 1.2.1.84). Further, described is the above method wherein the 3-methylbutyryl-CoA can be provided by the enzymatic conversion of 3-methylcrotonyl-CoA into said 3-methylbutyryl-CoA. It is also described that the thus obtained isoamyl alcohol can be further enzymatically converted into 3-methylbutyl acetate (isoamyl acetate) as described herein. Described are also recombinant organisms or microorganisms which are capable of performing the above enzymatic conversions. Furthermore, described are uses of enzymes and enzyme combinations which allow the above enzymatic conversions. 1. A method for the production of isoamyl alcohol (3-methylbutan-1-ol) comprising the enzymatic conversion of 3-methylbutyryl-CoA into isoamyl alcohol comprising: (i) first the enzymatic conversion of 3-methylbutyryl-CoA into 3-methylbutyraldehyde; and', '(ii) then enzymatically converting the thus obtained 3-methylbutyraldehyde into said isoamyl alcohol; or, '(a) two enzymatic steps comprising'}(b) a single enzymatic reaction in which 3-methylbutyryl-CoA is directly converted into isoamyl alcohol by making use of an alcohol-forming short chain acyl-CoA dehydrogenase/fatty acyl-CoA reductase or an alcohol-forming fatty acyl-CoA reductase (long-chain acyl-CoA:NADPH ...

Recombinant Engineered Bacterium Co-Expressing Trans-Anethole Oxygenase and Formate Dehydrogenase and Application thereof in Production of Piperonal

The present application discloses a method for producing piperonal by using a recombinant engineered bacterium co-expressing trans-anethole oxygenase and formate dehydrogenase, and an engineered bacterium thereof, including constructing a formate dehydrogenase gene fdh and trans-anethole oxygenase gene tao or trans-anethole oxygenase mutant gene co-expression recombinant vector; inductively expressing recombinant genetically engineered bacterium; and producing piperonal by using the recombinant genetically engineered bacterium. 15.91 g/L of piperonal with a transformation rate of 79.55% and a time-space transformation rate of 2.27 g/L/h can be finally obtained during catalysis, and the yield is significantly improved compared with the existing piperonal, thereby being more conducive to the smooth realization of industrial production.

Engineered CO2-Fixing Chemotrophic Microorganisms Producing Carbon-Based Products and Methods of Using the Same

Disclosed herein are microorganisms containing exogenous or heterologous nucleic acid sequences, wherein the microorganisms are capable of growing on gaseous carbon dioxide, gaseous hydrogen, syngas, or combinations thereof. In some embodiments the microorganisms are chemotrophic bacteria that produce or secrete at least 10% of lipid by weight. Also disclosed are methods of fixing gaseous carbon into organic carbon molecules useful for industrial processes. Also disclosed are methods of manufacturing chemicals or producing precursors to chemicals useful in jet fuel, diesel fuel, and biodiesel fuel. Exemplary chemicals or precursors to chemicals useful in fuel production are alkanes, alkenes, alkynes, fatty acid alcohols, fatty acid aldehydes, desaturated hydrocarbons, unsaturated fatty acids, hydroxyl acids, or diacids with carbon chains between six and thirty carbon atoms long. Also disclosed are microorganisms and methods using disclosed microorganisms for the production of butanediol and its chemical precursors in low-oxygen or anaerobic fermentation. Also disclosed are microorganisms and methods using disclosed microorganisms for generating hydroxylated fatty acids in microbes through the transfer of enzymes that are known to hydroxylate fatty acids in plants or microbes. Also disclosed are microorganisms and methods using disclosed microorganisms for the production of shorter-chain fatty acids in microbes through the introduction of exogenous fatty acyl-CoA binding proteins.

RECOMBINANT HOST CELLS AND PROCESSES FOR PRODUCING 1,3-BUTADIENE THROUGH A CROTONOL INTERMEDIATE

The present disclosure relates to recombinant host cells comprising one or more recombinant polynucleotides encoding enzymes in select pathways that provide the ability to use the cells to produce 1,3-butadiene. The present disclosure also provides methods of manufacturing the recombinant host cells, and methods for the use of the cells to produce 1,3-butadiene, either through formation of the intermediate compound crotonol followed by chemo-catalytic dehydration to 1,3-butadiene, or through the use of a recombinant cell comprising a fully enzymatic pathway capable of converting crotonyl-CoA or crotonyl-ACP to crotonol and then crotonol to 1,3-butadiene. 1. A recombinant host cell capable of producing crotonol , the host cell comprising:(a) a recombinant polynucleotide encoding a FAR enzyme capable of converting crotonyl-CoA and/or crotonyl-ACP to crotonol.2. The recombinant host cell of claim 1 , wherein the host cell further is capable of producing 1 claim 1 ,3-butadiene and further comprises:(b) a recombinant polynucleotide encoding an enzyme capable of converting crotonol to but-2-enyl phosphate; and(c) a recombinant polynucleotide encoding an enzyme capable of converting but-2-enyl phosphate to 1,3-butadiene.3. The recombinant host cell of claim 1 , wherein the recombinant polynucleotide encoding the FAR enzyme comprises one or more nucleotide sequence differences relative to the corresponding naturally occurring polynucleotide claim 1 , which result in an improved property selected from:(a) increased activity of the FAR enzyme in the conversion of crotonyl-CoA and/or crotonyl-ACP to crotonol;(b) increased expression of the FAR enzyme;(c) increased host cell tolerance of acetyl-CoA, acetoacetyl-CoA, malonyl-CoA, malonyl-ACP, 3-hydroxybutyryl-CoA, acetoacetyl-ACP, crotonyl-CoA, crotonyl-ACP, crotonol, but-2-enyl phosphate, or 1,3-butadiene; or(d) altered host cell concentration of acetyl-CoA, acetoacetyl-CoA, malonyl-CoA, malonyl-ACP, 3-hydroxybutyryl-CoA, ...

Novel 7Beta-Hydroxysteroid Dehydrogenase Mutants and Process for the Preparation of Ursodeoxycholic Acid

The invention relates to novel 7β-hydroxysteroid dehydrogenase mutants, to the sequences which encode these enzyme mutants, to processes for the preparation of the enzyme mutants and to their use in enzymatic reactions of cholic acid compounds, in particular in the preparation of ursodeoxycholic acid (UDCS). The invention also relates to novel processes for the synthesis of UDCS using the enzyme mutants; and to the preparation of UDCS using recombinant, multiply-modified microorganisms.

Mutant Microorganism Comprising Gene Encoding Methylmalonyl-CoA Reductase and Use Thereof

Provided herein is a mutant microorganism containing a methylmalonyl-CoA reductase-encoding gene having an activity of converting methylmalonyl-CoA to methylmalonate semialdehyde and uses of the mutant microorganism. The mutant microorganism includes a gene encoding kingdom Archaea-derived methylmalonyl-CoA reductase. 1. A mutant microorganism derived from a microorganism having the ability to produce succinyl-CoA from a carbon source , wherein the mutant microorganism contains genes encoding the following enzymes and has the ability to produce 3-HIBA (3-hydroxyisobutyric acid):(i) methylmalonyl-CoA mutase;(ii) methylmalonyl-CoA epimerase;(iii) methylmalonyl-CoA reductase; and(iv) 3-hydroxyisobutyrate dehydrogenase, wherein the enzyme of (iii) is an enzyme exhibiting methylmalonyl-CoA reductase activity among enzymes having malonyl-CoA reductase activity.2. The mutant microorganism of claim 1 , wherein enzyme (iii) is a monofunctional enzyme exhibiting methylmalonyl-CoA reductase activity and conversion activity methylmalonyl-CoA to methylmalonate semialdehyde claim 1 , selected from among enzymes having malonyl-CoA reductase activity.3. The mutant microorganism of claim 1 , wherein the enzyme exhibiting methylmalonyl-CoA reductase activity among enzymes having malonyl-CoA reductase activity is derived from an organism in kingdom Archae.4. The mutant microorganism of claim 3 , wherein enzyme (iii) is derived from one or more Archaea species selected from the group consisting of Candidatus Caldiarchaeum subterraneum claim 3 , Sulfolobales archaeon Acd1 claim 3 , and Sulfolobus acidocaldarius Ron12/I.5. The mutant microorganism of claim 1 , wherein enzyme (iii) comprises a sequence having a sequence homology of at least 60% SEQ ID NO: 23.6. The mutant microorganism of claim 1 , wherein the enzyme of (iii) comprises a sequence having a sequence homology of at least 60% to the sequence represented by any one selected from the group consisting of SEQ ID NO: 3 claim 1 , ...

METHODS FOR REGULATING NITROGEN METABOLISM DURING THE PRODUCTION OF ETHANOL FROM CORN BY METABOLICALLY ENGINEERED YEAST STRAINS

The present invention provides for a mechanism to reduce glycerol production and increase nitrogen utilization and ethanol production of recombinant microorganisms. One aspect of this invention relates to strains of with reduced glycerol productivity that get a kinetic benefit from higher nitrogen concentration without sacrificing ethanol yield. A second aspect of the invention relates to metabolic modifications resulting in altered transport and/or intracellular metabolism of nitrogen sources present in com mash.

Method for n-butanol production using heterologous expression of anaerobic pathways

The present invention relates to a method for the production of n-butanol using a transgenic cell with heterologous expression of 2-hydroxyglutarate dehydrogenase, glutaconate-CoA transferase, (R)-2-hydroxyglutaryl-CoA dehydrogenase, glutaryl CoA dehydrogenase, trans-2-enoyl-CoA reductase (NAD+) and bifunctional aldehyde/alcohol dehydrogenase (NAD+).

MODULATION OF THE GUT MICROBIOME TO TREAT MENTAL DISORDERS OR DISEASES OF THE CENTRAL NERVOUS SYSTEM

The present disclosure relates to methods of treating at least one symptom of a mental disorder or disease of the central nervous system in a subject by modulating the amount of GABA produced in the subject's gut. The present disclosure also relates to methods of culturing the bacterial strain new bacterial strains. Also disclosed are methods of identifying bacterial strains capable of producing GABA, and engineering strains to produce GABA. 1. A method of treating a disease or disorder in a subject in need thereof , the method comprising administering to the subject a therapeutic composition comprising at least one purified bacterial population that produces GABA at a pH range of between 4.5 and 7.5 , the at least one purified bacterial population consisting of bacteria comprising a 16s rDNA sequence at least 98% identical to a 16s rDNA sequence selected from the group consisting of SEQ ID NOs: 1-4 , 8 , 10 , 12 , 16-18 , 28-29 and 81.2. The method of claim 1 , wherein the at least one bacterial population consists of bacteria comprising a 16S rDNA sequence at least 99% identical to a 16S rDNA sequence selected from the group consisting of SEQ ID NOs: 1-4 claim 1 , 8 claim 1 , 10 claim 1 , 12 claim 1 , 16-18 claim 1 , 28-29 and 81.3. The method of claim 1 , wherein the disease or disorder is a mental disease or disorder.4. The method of claim 3 , wherein the mental disease or disorder is selected from the group consisting of depression claim 3 , bipolar disorder claim 3 , schizophrenia claim 3 , anxiety claim 3 , anxiety disorders claim 3 , addiction claim 3 , social phobia claim 3 , treatment-resistant major depressive disorder (TR-MDD) claim 3 , major depressive disorder and its subtypes claim 3 , neurodegenerative amyloid disorders claim 3 , orthostatic tremor claim 3 , Lafora disease claim 3 , restless leg syndrome claim 3 , neuropathic pain claim 3 , pain disorders claim 3 , dementia claim 3 , epilepsy claim 3 , stiff-person syndrome claim 3 , premenstrual ...

Atp driven direct photosynthetic production of fuels and chemicals

Provided herein are metabolically-modified microorganisms useful for producing biofuels. More specifically, provided herein are methods of producing high alcohols including isobutanol, 1-butanol, 1-propanol, 2-methyl-l-butanol, 3-methyl-1-butanol and 2-phenylethanol from a suitable substrate.

BUTYRALDEHYDE DEHYDROGENASE MUTANT, POLYNUCLEOTIDE ENCODING THE MUTANT, VECTOR AND MICROORGANISM HAVING THE POLYNUCLEOTIDE, AND METHOD OF PRODUCING 1,4-BUTANEDIOL USING THE SAME

A mutant butyraldehyde dehydrogenase (Bld), a polynucleotide having a nucleotide encoding the mutant, a vector including the polynucleotide, a microorganism including a nucleotide encoding the mutant, and a method of producing 1,4-butanediol using the same. 1. A butyraldehyde dehydrogenase that converts 4-hydroxybutyryl CoA to 4-hydroxybutyraldehyde comprising the amino acid sequence of SEQ ID NO: 1 with a mutation of at least one amino acid residue at an NADH or NADPH binding site.2. The butyraldehyde dehydrogenase of claim 1 , wherein one or more of Gly226 claim 1 , Met227 claim 1 , or Leu273 of SEQ ID NO: 1 is substituted with another amino acid.3. The butyraldehyde dehydrogenase of claim 2 , wherein Gly226 of SEQ ID NO: 1 is substituted with Ile claim 2 , Leu claim 2 , Phe claim 2 , or Tyr.4. The butyraldehyde dehydrogenase of claim 2 , wherein Met227 of SEQ ID NO: 1 is substituted with Ile claim 2 , Leu claim 2 , Gln claim 2 , or Val.5. The butyraldehyde dehydrogenase of claim 2 , wherein Leu273 of SEQ ID NO: 1 is substituted with Ile.6. The butyraldehyde dehydrogenase of claim 2 , wherein Leu273 of SEQ ID NO: 1 is substituted with Ile and Met227 of SEQ ID NO: 1 is substituted with Ile claim 2 , Leu claim 2 , Gln claim 2 , or Val.7. The butyraldehyde dehydrogenase of claim 1 , wherein the NADH or NADPH binding site comprises the 226 claim 1 , 227 claim 1 , and 273amino acid residues of SEQ ID NO: 1.8. The butyraldehyde dehydrogenase of claim 1 , comprising a polypeptide selected from the group consisting of SEQ ID NO: 3 to SEQ ID NO: 9.9. A recombinant microorganism comprising a polynucleotide encoding the butyraldehyde dehydrogenase of .10. The recombinant microorganism of claim 9 , wherein the microorganism converts 4-hydroxybutyryl CoA to 4-hydroxybutyraldehyde at an increased level relative to a non-recombinant microorganism.11. The recombinant microorganism of claim 9 , wherein the microorganism further comprises a polynucleotide encoding a polypeptide ...

COMPOSITIONS AND METHODS FOR THE BIOSYNTHESIS OF 1,4-BUTANEDIOL AND ITS PRECURSORS

The invention provides a non-naturally occurring microbial biocatalyst including a microbial organism having a 4-hydroxybutanoic acid (4-HB) biosynthetic pathway having at least one exogenous nucleic acid encoding 4-hydroxybutanoate dehydrogenase, succinyl-CoA synthetase, CoA-dependent succinic semialdehyde dehydrogenase, or α-ketoglutarate decarboxylase, wherein the exogenous nucleic acid is expressed in sufficient amounts to produce monomeric 4-hydroxybutanoic acid (4-HB). Also provided is a non-naturally occurring microbial biocatalyst including a microbial organism having 4-hydroxybutanoic acid (4-HB) and 1,4-butanediol (BDO) biosynthetic pathways, the pathways include at least one exogenous nucleic acid encoding 4-hydroxybutanoate dehydrogenase, succinyl-CoA synthetase, CoA-dependent succinic semialdehyde dehydrogenase, 4-hydroxybutyrate:CoA transferase, 4-butyrate kinase, phosphotransbutyrylase, α-ketoglutarate decarboxylase, aldehyde dehydrogenase, alcohol dehydrogenase or an aldehyde/alcohol dehydrogenase, wherein the exogenous nucleic acid is expressed in sufficient amounts to produce 1,4-butanediol (BDO). Additionally provided is a method for the production of 4-HB. The method includes culturing a non-naturally occurring microbial organism having a 4-hydroxybutanoic acid (4-HB) biosynthetic pathway including at least one exogenous nucleic acid encoding 4-hydroxybutanoate dehydrogenase, succinyl-CoA synthetase, CoA-dependent succinic semialdehyde dehydrogenase or α-ketoglutarate decarboxylase under substantially anaerobic conditions for a sufficient period of time to produce monomeric 4-hydroxybutanoic acid (4-HB). Further provided is a method for the production of BDO. The method includes culturing a non-naturally occurring microbial biocatalyst, comprising a microbial organism having 4-hydroxybutanoic acid (4-HB) and 1,4-butanediol (BDO) biosynthetic pathways, the pathways including at least one exogenous nucleic acid encoding 4-hydroxybutanoate ...

MICROORGANISMS AND METHODS FOR THE CO-PRODUCTION OF ETHYLENE GLYCOL AND THREE CARBON COMPOUNDS

The present application relates to recombinant microorganisms useful in the biosynthesis of monoethylene glycol (MEG) and one or more three-carbon compounds such as acetone, isopropanol or propene. The MEG and one or more three-carbon compounds described herein are useful as starting material for production of other compounds or as end products for industrial and household use. The application further relates to recombinant microorganisms co-expressing a C2 branch pathway and a C3 branch pathway for the production of MEG and one or more three-carbon compounds. Also provided are methods of producing MEG and one or more three-carbon compounds using the recombinant microorganisms, as well as compositions comprising the recombinant microorganisms and/or optionally the products MEG and one or more three-carbon compounds. 2. The recombinant microorganism of claim 1 , wherein the recombinant microorganism further comprises at least one endogenous or exogenous nucleic acid molecule encoding a secondary alcohol dehydrogenase that catalyzes the conversion of acetone to isopropanol.3. The recombinant microorganism of claim 1 , wherein the recombinant microorganism further comprises: at least one endogenous or exogenous nucleic acid molecule encoding a secondary alcohol dehydrogenase that catalyzes the conversion of acetone to isopropanol; and at least one endogenous or exogenous nucleic acid molecule encoding a dehydratase that catalyzes the conversion of isopropanol to propene.4. The recombinant microorganism of claim 1 , wherein the recombinant microorganism further comprises one or more modifications selected from the group consisting of:(a) a deletion, insertion, or loss of function mutation in a gene encoding a D-xylose isomerase that catalyzes the conversion of D-xylose to D-xylulose;(b) a deletion, insertion, or loss of function mutation in a gene encoding a glycolaldehyde dehydrogenase that catalyzes the conversion of glycolaldehyde to glycolic acid; and(c) a deletion, ...

MATERIALS AND METHODS FOR DIRECTING CARBON FLUX AND INCREASED PRODUCTION OF CARBON BASED CHEMICALS

This disclosure relates to genome-scale attenuation or knockout strategies for directing carbon flux to certain carbon based building blocks within the 7-aminoheptanoic acid (7-AHA) and 6-aminohexanoic acid (6-AHA) biosynthesis pathways, for example, to achieve reduced flux to unwanted side products while achieving increased production of desired intermediates and end products. This disclosure also relates to non-naturally occurring mutant bacterial strains comprising one or more gene disruptions in aldehyde reductase and/or aldehyde dehydrogenase genes that are generated to direct carbon flux to certain carbon based building blocks. This disclosure further relates to a method for enhancing production of carbon based building blocks by generating non-naturally occurring mutant bacterial strains, culturing said mutant bacterial strains in the presence of suitable substrates or under desired growth conditions, and substantially purifying the desired end product. 1. A method for enhancing biosynthesis of 7-aminoheptanoic acid or 6-aminohexanoic acid comprising:a) generating a recombinant host comprising one or more gene disruptions in aldehyde reductase and/or aldehyde dehydrogenase genes, wherein said gene disruptions reduce aldehyde reductase and/or aldehyde dehydrogenase activity of polypeptides encoded by said genes, and wherein said recombinant host produces an increased level of 7-aminoheptanoic acid or 6-aminohexanoic acid converted from pimelic acid or pimelic acid derivatives or adipic acid or adipic acid derivatives as compared to a wild-type recombinant host;b) culturing said recombinant host in the presence of a suitable substrate or metabolic intermediate and under conditions suitable for the conversion of pimelic acid or pimelic acid derivatives to 7-aminoheptanoic acid or adipic acid or adipic acid derivatives to 6-aminohexanoic acid; andc) obtaining the 7-aminoheptanoic acid or 6-aminohexanoic acid.2. The method of claim 1 , wherein said pimelic acid ...

Genetically Modified Cell and Process for Use of Said Cell

The present invention relates to the field of biotransformation of furanic compounds. More particular the present invention relates to novel genetically modified cells with improved characteristics for biocatalytic transformation of furanic compounds and a vector suitable for the genetic modification of a host cell. Further aspects of the invention are aimed at processes for biotransformation of 5-(hydroxymethyl)furan-2-carboxylic acid (HMF-acid) and its precursors with the use of the cell according to the invention. 124-. (canceled)25. A process for producing 2 ,5-furandicarboxylic acid (FDCA) , the process comprising the step of incubating a cell in the presence of one or more furanic precursors of HMF-acid under conditions suitable for the oxidation by said cell of the one or more furanic precursors to FDCA , wherein said conditions include that the cell is incubated at a pH from pH 1 to 6 , and wherein the cell is genetically modified to express a polynucleotide sequence coding for a polypeptide having HMF-acid oxidoreductase activity.26. The process of claim 25 , wherein the cell is incubated at a pH from pH 1 to 4.27. The process of claim 26 , wherein the cell is incubated at a pH from pH 1 to 3.28. The process of claim 25 , wherein the cell is a fungal cell.29Candida, Hansenula, Kluyveromyces, Pichia, Saccharomyces, Schizosaccharomyces, Yarrowia, Acremonium, Agaricus, Aspergillus, Aureobasidium, Chrysosporium, Coprinus, Cryptococcus, Filibasidium, Fusarium, Humicola, Magnaporthe, Mucor, Myceliophthora, Neocallimastix, Neurospora, Paecilomyces, Penicillium, Piromyces, Phanerochaete, Pleurotus, Schizophyllum, Talaromyces, Thermoascus, Thielavia, TolypocladiumTrichoderma.. The process of claim 28 , wherein the cell belongs to a fungal genus selected from the group consisting of the genera and30Kluyveromyces lactis, Saccharomyces cerevisiae, Hansenula polymorpha, Yarrowia lipolytica, Pichia stipitis, Pichia pastoris, Aspergillus niger, Aspergillus awamori, ...

Compositions and methods for converting styrene to biodegradable alternatives

Provided are nucleic acids and vectors that collectively encode various gene products related to converting styrene to polyhydroxybutyrate (PHB). In some embodiments, the nucleic acids and vectors collectively encode a styrene monooxygenase polypeptide, a flavin reductase polypeptide, a styrene-oxide isomerase polypeptide, and a phenylacetaldehyde dehydrogenase polypeptide, an acetyl-CoA C-acetyltransferase polypeptide, a 3-ketoacyl-ACP reductase polypeptide, a class I poly(R)-hydroxyalkanoic acid synthase polypeptide, and optionally an influx porin polypeptide. Also provided are systems and methods for producing PHB from styrene, methods and systems for remediating polystyrene waste. In some embodiments, the systems are in vivo systems.

Microorganisms of the genus corynebacterium having l-isoleucine producing ability and methods for producing l-isoleucine using the same

The present application relates to a microorganism of the genus Corynebacterium having L-isoleucine producing ability which comprises a protein having an activity of citramalate synthase, and a method for producing L-isoleucine using the same.

RECOMBINANT MICROORGANISM HAVING ABILITY TO PRODUCE POLY(LACTATE-COGLYCOLATE) OR COPOLYMER THEREOF FROM XYLOSE AND METHOD FOR PREPARING POLY(LACTATE-COGLYCOLATE) OR COPOLYMER THEREOF BY USING SAME

The present invention relates to a recombinant microorganism having the ability to produce poly(lactate-co-glycolate) and its copolymers from xylose, and more particularly to a recombinant microorganism having the ability to produce poly(lactate-co-glycolate) and its copolymers without having to supply a glycolate precursor from an external source, and a method of producing a poly(lactate-co-glycolate) copolymers using the same. 1. A recombinant microorganism having the ability to produce poly(lactate-co-glycolate) , wherein a polyhydroxyalkanoate synthase-encoding gene , a propionyl-CoA transferase-encoding gene , a xylose dehydrogenase-encoding gene , and a xylonolactonase-encoding gene are introduced in a microorganism having the ability to produce lactate from pyruvic acid.2Pseudomonas. The recombinant microorganism of claim 1 , wherein the polyhydroxyalkanoate synthase is PHA synthase derived from sp. 6-19 or a mutant enzyme of PHA synthase claim 1 , which has an amino acid sequence selected from the following amino acid sequences:an amino acid sequence comprising at least one mutation selected from the group consisting of E130D, S325T, S477G, S477F, S477Y, S477G and Q481K in the amino acid sequence of SEQ ID NO: 1;an amino acid sequence (PhaC1202) comprising mutations of E130D and Q481K in the amino acid sequence of SEQ ID NO: 1;an amino acid sequence (PhaC1301) comprising mutations of E130D, S325T and Q481K in the amino acid sequence of SEQ ID NO: 1;an amino acid sequence (PhaC1310) comprising mutations of E130D, S477F and Q481K in the amino acid sequence of SEQ ID NO: 1;an amino acid sequence (PhaC1437) comprising mutations of E130D, S325T, S477G and Q481K in the amino acid sequence of SEQ ID NO: 1; andan amino acid sequence (PhaC1439) comprising mutations of E130D, S325T, S477F and Q481K in the amino acid sequence of SEQ ID NO: 1.3. The recombinant microorganism of claim 1 , wherein the propionyl-CoA transferase is a Pct540 enzyme having the amino acid ...

Gold Optimized CAR T-cells

Control Devices are disclosed including RNA destabilizing elements (RDE), RNA control devices, and destabilizing elements (DE) combined with Chimeric Antigen Receptors (CARs) or other transgenes in eukaryotic cells. Multicistronic vectors are also disclosed for use in engineering host eukaryotic cells with the CARs and transgenes under the control of the control devices. These control devices can be used to optimize expression of CARs in the eukaryotic cells so that, for example, effector function is optimized. CARs and transgene payloads can also be engineered into eukaryotic cells so that the transgene payload is expressed and delivered after stimulation of the CAR on the eukaryotic cell. 1. (canceled)2. (canceled)3. (canceled)4. (canceled)5. (canceled)6. (canceled)7. (canceled)8. (canceled)9. (canceled)10. (canceled)11. (canceled)12. (canceled)13. (canceled)14. (canceled)15. (canceled)16. (canceled)17. (canceled)18. (canceled)19. (canceled)20. (canceled)21. A method for expressing a transgene , comprising the steps of:(a) obtaining an immune cell comprising a chimeric antigen receptor, and a heterologous nucleic acid comprising a polynucleotide encoding the transgene that is operably linked to a polynucleotide encoding a RDE, wherein the heterologous nucleic acid is transcribed to make a transcript encoding the transgene operably linked to the RDE, wherein an RDE binding protein binds to the RDE and regulates expression of the transgene;(b) binding the immune cell to a target ligand for the receptor at a target site in a subject wherein binding of the target ligand by the chimeric antigen receptor activates the immune cell, wherein activation of the immune cell changes binding of the RDE by the RDE binding protein; and(c) expressing the transgene wherein the amount of polypeptide made from the transgene is increased after activation of the cell by the receptor.22. The method of claim 1 , wherein the immune cell is a T-cell.23. The method of wherein the transgene ...

Constructs and systems and methods for producing microcompartments

To produce a bacterial microcompartment shell, or a designed shell based on naturally occurring bacterial microcompartment shells in a new host organism, a synthetic operon is constructed that contains the desired shell protein genes and translation efficiency is controlled by host specific ribosomal binding sites. Proteins or other molecules can be encapsulated in the microcompartment shells by various methods described herein. The constructs can also be used to express self-assembling sheets comprised of shell proteins.

IMPROVED GLYCEROL FREE ETHANOL PRODUCTION

The invention relates to a recombinant cell, preferably a yeast cell comprising one or more genes coding for an enzyme having glycerol dehydrogenase activity, one or more genes coding dihydroxyacetone kinase (E.C. 2.7.1.28 and/or E.C. 2.7.1.29); one or more genes coding for an enzyme in an acetyl-CoA-production pathway and one or more genes coding for an enzyme having at least NAD dependent acetylating acetaldehyde dehydrogenase activity (EC 1.2.1.10 or EC 1.1.1.2), and optionally one or more genes coding for a glycerol transporter. This cell can be used for the production of ethanol and advantageously produces little or no glycerol. 1. A recombinant cell , optionally a yeast cell , said recombinant cell comprising:one or more genes coding for an enzyme having glycerol dehydrogenase activity;one or more genes coding dihydroxyacetone kinase (E.C. 2.7.1.28 and/or E.C. 2.7.1.29);one or more genes coding for an enzyme in an acetyl-CoA-production pathway; and{'sup': '+', 'one or more genes coding for an enzyme having at least NAD dependent acetylating acetaldehyde dehydrogenase activity (EC 1.2.1.10 or EC 1.1.1.2); and optionally'}one or more genes coding for a glycerol transporter.2. The Cell according to wherein the enzyme having glycerol dehydrogenase activity is a NAD linked glycerol dehydrogenase (EC 1.1.1.6).3. The Cell according to wherein the enzyme having glycerol dehydrogenase activity is a NADP linked glycerol dehydrogenase (EC 1.1.1.72).4. The recombinant cell according to wherein the one or more genes coding for an enzyme in an acetyl-CoA-production pathway comprises:one or more genes coding for an enzyme having phosphoketolase (PKL) activity (EC 4.1.2.9 or EC 4.1.2.22) or an enzyme having an amino acid sequence according SEQ ID NO: 5, 6, 7, or 8, or functional homologues thereof having a sequence identity of at least 50%, and/orone or more genes coding for an enzyme having phosphotransacetylase (PTA) activity (EC 2.3.1.8) or an enzyme having an amino acid ...

Engineered microbes for conversion of organic compounds to medium chain length alcohols and methods of use

This disclosure provides a genetically-modified bacterium from the genus Pseudomonasthat comprises an exogenous nucleic acid encoding an enoyl-CoA reductase and an exogenous nucleic acid encoding an acyl-CoA reductase that produces medium chain length alcohols. The disclosure further provides methods for producing medium chain alcohols using such genetically-modified bacterium. This disclosure provides a renewable, bio-based production platform for valuable mcl-alcohols that have a wide range of industrial applications. Current production of mcl-alcohols typically occurs through the hydrogenation of plant oils and waxes. This process leads to issues of deforestation and is largely unsustainable. Utilizing waste lignin streams as the carbon source provides a more sustainable feedstock that can be generated from plant waste like corn stover. Along with this, the use of lignin avoids competition with food resources as traditional starch and sugar feedstocks.

ENGINEERED MICROBES FOR CONVERSION OF ORGANIC COMPOUNDS TO BUTANOL AND METHODS OF USE

This disclosure provides a genetically-modified bacterium from the genus that comprises an exogenous nucleic acid encoding a bifunctional aldehyde/alcohol dehydrogenase that produces butanol as the final product. The disclosure further provides methods for producing butanol using such genetically-modified bacterium. 1Megasphaera. A genetically-modified bacterium from the genus , comprising an exogenous nucleic acid encoding a bifunctional aldehyde/alcohol dehydrogenase wherein the bifunctional aldehyde/alcohol dehydrogenase produces butanol as a final product.2Clostridium.. The genetically-modified bacterium of claim 1 , wherein the bifunctional aldehyde/alcohol dehydrogenase is an enzyme from a bacterial species that belongs to the genus3. The genetically-modified bacterium of claim 2 , wherein the bifunctional aldehyde/alcohol dehydrogenase comprises an amino acid sequence with at least 90% identity to SEQ ID NO: 1.4Megasphaera. The genetically-modified bacterium of claim 1 , wherein the exogenous nucleic acid sequence is codon optimized for the species of the genus to which the genetically modified bacterium belongs.5MegasphaeraM. hominis, M. cerevisiae, M. elsdenii, M. micronuciformis, M. paucivoransM. sueciensis. The genetically-modified bacterium of claim 1 , wherein the genetically-modified bacterium is from a species selected from the group consisting of claim 1 , and6M. elsdeni.. The genetically-modified bacterium of claim 5 , wherein the genetically-modified bacterium is from the species7M. elsdenii. The genetically-modified bacterium of claim 6 , wherein the genetically-modified bacterium is an strain designated as ATCC 25940.8Megasphaera. A method for converting an organic compound to butanol claim 6 , the method comprising inoculating a medium comprising said organic compound with a genetically-modified bacterium from the genus claim 6 , wherein the bacterium comprises an exogenous nucleic acid encoding a bifunctional aldehyde/alcohol dehydrogenase ...

E1 ENZYME MUTANTS AND USES THEREOF

The invention provides isolated nucleic acids molecules, designated UBA3, UAE, or UBA6, or other E1 enzyme variant nucleic acid molecules, which encode novel E1 enzyme variant proteins. The invention also provides antisense nucleic acid molecules, recombinant expression vectors containing UBA3, UAE, or UBA6, or other E1 enzyme variant nucleic acid molecules, host cells into which the expression vectors have been introduced, and nonhuman transgenic animals in which a UBA3, UAE, or UBA6, or other E1 enzyme variant gene has been introduced or disrupted. The invention still further provides isolated UBA3, UAE, or UBA6, or other E1 enzyme variant proteins, fusion proteins, antigenic peptides and anti-UBA3, UAE, or UBA6, or other E1 enzyme variant antibodies. The invention provides methods to identify agents that inhibit UBA3, UAE, or UBA6, or other E1 enzyme variant expression or activity. Diagnostic and therapeutic methods utilizing compositions of the invention are also provided. 132.-. (canceled)33. An isolated E1 enzyme variant polypeptide selected from the group consisting of:a) a UBA3 variant polypeptide comprising a variant of the amino acid sequence of SEQ ID NO:2, wherein the variant has a mutation of the amino acid selected from the group consisting of amino acid residue 171, 201, 204, 205, 209, 211, 228, 229, 249, 305, 311, 314 and 324;b) a UBA3 variant polypeptide comprising a fragment of a variant of the amino acid sequence of SEQ ID NO:2, wherein the fragment comprises at least 15 contiguous amino acids of SEQ ID NO: 2, and wherein the fragment has a mutation of the amino acid selected from the group consisting of amino acid residue 171, 201, 204, 205, 209, 211, 228, 229, 249, 305, 311, 314 and 324;c) a polypeptide comprising an amino acid sequence selected from the group consisting of: an SAE2 variant of SEQ ID NO:27 with a mutation at residue 121, a UBA1 variant of SEQ ID NO:28 with a mutation at residue 548, a UBA1 variant of SEQ ID NO:29, with a ...

Fermentive Production of Four Carbon Alcohols

Methods for the fermentative production of four carbon alcohols is provided. Specifically, butanol, preferably isobutanol is produced by the fermentative growth of a recombinant bacterium expressing an isobutanol biosynthetic pathway. 182-. (canceled)84. The method of claim 83 , further comprising recovering the bioproduced isobutanol.85. The method of claim 84 , further comprising removing solids from the fermentation medium.86. The method of claim 84 , wherein the recovering is by distillation claim 84 , liquid-liquid extraction claim 84 , adsorption claim 84 , decantation claim 84 , pervaporation claim 84 , or combinations thereof.87. The method of claim 85 , wherein the removing is by centrifugation claim 85 , filtration claim 85 , or decantation.88. The method of claim 85 , wherein the removing occurs before the recovering. This application is a continuation of and claims priority to U.S. patent application Ser. No. 14/715,992, filed May 19, 2015 which is a continuation of and claims priority to U.S. patent application Ser. No. 13/539,125, now U.S. Pat. No. 9,068,190, filed on Jun. 29, 2012 which is a continuation of and claims priority to U.S. patent application Ser. No. 12/939,284, now U.S. Pat. No. 8,283,144, filed on Nov. 4, 2010 which is a continuation of and claims priority to U.S. patent application Ser. No. 11/586,315, now U.S. Pat. No. 7,851,188, filed on Oct. 25, 2006, which claims priority under 35 U.S.C. §119 from U.S. Provisional Application Ser. No. 60/730,290, filed Oct. 26, 2005.The invention relates to the field of industrial microbiology and the production of alcohols. More specifically, isobutanol is produced via industrial fermentation of a recombinant microorganism.Butanol is an important industrial chemical, useful as a fuel additive, as a feedstock chemical in the plastics industry, and as a foodgrade extractant in the food and flavor industry. Each year 10 to 12 billion pounds of butanol are produced by petrochemical means and the need ...

ENGINEERING OF HYDROCARBON METABOLISM IN YEAST

The present invention relates to the development of genetically engineered yeasts that can produce hydrocarbons in a controllable and economic fashion. More specifically the invention relates to the production of liquid alkanes and alkenes that can be used for liquid transportation fuels, specialty chemicals, or feed stock for further chemical conversion. 130-. (canceled)31. A yeast , whereinsaid yeast lacks a gene encoding hexadecanal dehydrogenase (HFD1) or comprises a disrupted gene encoding HFD1; andsaid yeast comprises at least one heterologous gene encoding an enzyme involved in a pathway of producing fatty acids or fatty acid derivatives.32. The yeast according to claim 31 , wherein the fatty acids or fatty acid derivatives are fatty alcohols and/or fatty aldehydes.33. The yeast according to claim 31 , wherein said yeast comprises at least one heterologous gene encoding an enzyme involved in a pathway of producing fatty acid derivatives from fatty acyl-Coenzyme A (CoA) through fatty aldehydes.34. The yeast according to claim 31 , wherein the at least one heterologous gene encoding an enzyme involved in a pathway of producing fatty acids or fatty acid derivatives is a gene encoding carboxylic acid reductase.35Mycobacterium marinum.. The yeast according to claim 34 , wherein the gene encoding carboxylic acid reductase is from36. The yeast according to claim 34 , further comprising a gene encoding a phosphopantetheinyl transferase.37Aspergillus nidulans.. The yeast accordingly to claim 36 , wherein the gene encoding a phosphopantetheinyl transferase is from38. The yeast according to claim 31 , wherein the at least one heterologous gene encoding an enzyme involved in a pathway of producing fatty acids or fatty acid derivatives is a heterologous gene encoding a thioesterase.39Escherichia coli. The yeast according to claim 38 , wherein the gene encoding a thioesterase is selected from the group consisting of tesA claim 38 , tesB claim 38 , fadM and yciA.40. The ...

DEHYDROGENASE-CATALYSED PRODUCTION OF FDCA

The invention relates to a cell expressing a polypeptide having 5-hydroxymethyl-2-furancarboxylic acid dehydrogenase activity, as well as to a cell expressing a polypeptide having furanic compound transport capabilities. The invention also relates to a process for the production of 2,5-furan-dicarboxylic acid (FDCA) wherein the cells of the invention are used for oxidation of a furanic precursors of FDCA. 115.-. (canceled)16. A process for oxidizing 5-hydroxymethyl-2-furancarboxylic acid (HMFCA) to 5-formyl-2-furoic acid (FFA) , the process comprising incubating a cell in the presence of HMFCA , wherein the cell comprises an expression construct for expression of a nucleotide sequence encoding an HMFCA dehydrogenase having an amino acid sequence with at least 45% identity with any one of the amino acid sequence of SEQ ID NO: 1 to 11 , and wherein , the expression construct is expressible in the cell and expression of the dehydrogenase confers to or increases in the cell the ability to oxidize HMFCA to FFA , as compared to a corresponding wild type cell lacking the expression construct.17. The process according to claim 16 , wherein the incubating is under conditions conducive to the oxidation of HMFCA by the cell.18. A process for producing FDCA claim 16 , comprising incubating a cell in a medium comprising one or more furanic precursors of FDCA claim 16 , and claim 16 , optionally recovery of the FDCA claim 16 , wherein the cell comprises an expression construct for expression of a nucleotide sequence encoding an HMFCA dehydrogenase having an amino acid sequence with at least 45% identity with any one of the amino acid sequence of SEQ ID NO: 1 to 11 claim 16 , wherein the expression construct is expressible in the cell and expression of the HMFCA dehydrogenase confers to or increases in the cell the ability to oxidize HMFCA to FFA claim 16 , as compared to a corresponding wild type cell lacking the expression construct.19. The process according to claim 18 , ...

A METHOD FOR UTILIZING ENGINEERED DENDRITIC CELLS TO INDUCE GUT-HOMING REGULATORY T CELLS AND TREAT GUT INFLAMMATION

Gene-modified, lymphoid-tissue-homing dendritic cells that comprise a 1-alpha-hydroxylase gene and a retinaldehyde dehydrogenase 2 gene, where the 1-alpha-hydroxylase gene is expressed to produce functional 1-alpha-hydroxylase enzyme and the retinaldehyde dehydrogenase 2 gene is expressed to produce functional retinaldehyde dehydrogenase 2 gene enzyme. A method for treating one or more than one inflammation-related condition or disease, the method comprising administering gene-modified, lymphoid-tissue-homing dendritic cells that comprise a 1-alpha-hydroxylase gene and a retinaldehyde dehydrogenase 2 gene, where the 1-alpha-hydroxylase gene is expressed to produce functional 1-alpha-hydroxylase enzyme and the retinaldehyde dehydrogenase 2 gene is expressed to produce functional retinaldehyde dehydrogenase 2 gene enzyme. 1. A gene-modified dendritic cell suitable for treating one or more than one inflammation-related condition or disease; the gene-modified dendritic cell comprising a 1-alpha-hydroxylase gene that produces functional 1-alpha-hydroxylase and a retinaldehyde dehydrogenase 2 gene that produces functional retinaldehyde dehydrogenase 2.2. The gene-modified dendritic cell of claim 1 , wherein the gene-modified dendritic cell is administered to a patient.3. The gene-modified dendritic cell of claim 2 , wherein after administration to the patient the gene-modified dendritic cell migrates into and actively produce 1 claim 2 ,25(OH)2D and retinoid acid in peripheral lymphoid organs.4. A pharmaceutical suitable for treating one or more than one inflammation-related condition or disease claim 2 , the pharmaceutical comprising:a gene-modified dendritic cell comprising a 1-alpha-hydroxylase gene that produces functional 1-alpha-hydroxylase and a retinaldehyde dehydrogenase 2 gene that produces functional retinaldehyde dehydrogenase 2.5. A method for treating one or more than one inflammation-related condition or disease claim 2 , the method comprises:identifying a ...

VACCINE FOR IMMUNOCOMPROMISED HOSTS

The invention provides peptides derived from a ubiquitous protein, and nucleic acids encoding such peptides. The invention extends to various uses of these peptides and nucleic acids, for example, as antigens for use in vaccines per se and in the generation of antibodies for use in therapeutic drugs for the prevention, amelioration or treatment of infections caused by sepsis-inducing bacteria. The invention particularly benefits immunocompromised hosts such as neonates, babies, children, women of fertile age, pregnant women, foetuses, the elderly and diabetics. 1. An isolated peptide that has at least 90% amino acid sequence identity with an amino acid sequence found within SEQ ID NO: 3 , and has less than 10% amino acid sequence identity with a peptide found within SEQ ID NO: 8 , wherein the isolated peptide is at least 8 amino acids and less than 50 amino acids in length and comprises an amino acid sequence that has at least 95% amino acid sequence identity to any one of SEQ ID NOs: 26-33.3. The isolated peptide of claim 1 , wherein the isolated peptide is conjugated to a carrier protein.4. The isolated peptide of claim 2 , wherein the isolated peptide is conjugated to a carrier protein. This application is a continuation application of U.S. application Ser. No. 15/313,327, filed Nov. 22, 2016, which is a U.S. National Phase patent application of PCT/EP2015/063243, filed Jun. 12, 2015, which claims priority to European Patent Applications No. 15398003.2, filed Mar. 30, 2015, and Ser. No. 14/398,006.8 filed Jun. 12, 2014, all of which are hereby incorporated by reference in the present disclosure in their entirety.The present invention relates to diseases, disorders and conditions caused by sepsis-inducing bacteria and particularly, although not exclusively, to the treatment and prevention of sepsis and sepsis-related pathologies. The invention extends to novel peptides and their encoding nucleic acids, and to the use of these peptides to create vaccines for the ...

DICARBOXYLIC ACID SYNTHESIS-RELATED ENZYME, AND METHOD FOR PRODUCING DICARBOXYLIC ACID USING SAME

The present invention elates to a dicarboxylic acid synthesis-related enzyme, a gene coding for same, and a method for producing dicarboxylic acid using same. The gene or enzyme encoded by the gene of the present invention can be used in bio-enzymatic production, instead of the existing chemical production, of dicarboxylic acid, and is thus expected to have high industrial utility. 1. A protein involved in the biosynthesis of a dicarboxylic acid (DCA) comprising one or more selected from a lipase (LIP1) , cytochrome P450 52B1 (CYP52B1) , an NADPH-cytochrome P450 reductase (NCP1) , a long-chain alcohol oxidase (FAO1) , and an aldehyde dehydrogenase (ALD1).2Candida tropicalis. The protein of claim 1 , wherein the proteins are derived from a strain.3. The protein of claim 1 , wherein the dicarboxylic acid is a C6-C20 dicarboxylic acid.4. The protein of claim 1 , wherein the lipase (LIP1) is expressed by a gene set forth in SEQ ID NO: 1; the cytochrome P450 52B1 (CYP52B1) is expressed by a gene set forth in SEQ ID NO: 2; the NADPH-cytochrome P450 reductase (NCP1) is expressed by a gene set forth in SEQ ID NO: 3; the long-chain alcohol oxidase (FAO1) is expressed by a gene set forth in SEQ ID NO: 4; and the aldehyde dehydrogenase (ALD1) is expressed by a gene set forth in SEQ ID NO: 5.5. A composition for biosynthesis of a dicarboxylic acid comprising a recombinant vector comprising one or more genes selected from the group consisting of a gene set forth in SEQ ID NO: 1; a gene set forth in SEQ ID NO: 2; a gene set forth in SEQ ID NO: 3; a gene set forth in SEQ ID NO: 4; and a gene set forth in SEQ ID NO: 5.6. A microorganism having an ability to produce a dicarboxylic acid (DCA) claim 5 , wherein the microorganism is transformed with the composition defined in .7Candida tropicalis. The microorganism of claim 6 , wherein the microorganism is a strain whose β-oxidation pathway is blocked.8. A method for producing a dicarboxylic acid (DCA) claim 6 , the method comprising ...

Enhanced Production Of Fatty Acid Derivatives

Genetically engineered cells and microorganisms are provided that produce products from the fatty acid biosynthetic pathway (fatty acid derivatives), as well as methods of their use. The products are particularly useful as biofuels. 1. A recombinant host cell comprising:at least one gene exogenous gene encoding a fatty acid derivative enzyme selected from: a thioesterase, an acyl-CoA synthase, an alcohol forming-CoA reductase, an acyl-CoA reductase, an ester synthase and an alcohol dehydrogenase.2. The recombinant cell of claim 1 , wherein the at least one exogenous gene encoding the fatty acid derivative enzyme is over-expressed.3. The recombinant host cell of claim 1 , wherein the recombinant host cell comprises at least one exogenous thioesterase gene.4. The recombinant host cell of claim 3 , wherein the at least one thioesterase gene encodes a thioesterase having EC number: EC 3.1.2.- or EC 3.1.1.5 or EC 3.1.2.14.5. The recombinant host cell of claim 1 , wherein the recombinant host cell comprises at least one exogenous thioesterase gene claim 1 , an exogenous acyl-CoA synthase gene and at least one exogenous gene selected from the group consisting of an exogenous an acyl-CoA reductase gene claim 1 , an exogenous alcohol dehydrogenase gene and an exogenous fatty alcohol forming acyl-CoA reductase gene.6. The recombinant host cell of claim 5 , wherein the at least one thioesterase is: a thioesterase having EC number: EC 3.1.2.- or EC 3.1.1.5 or EC 3.1.2.14.7. The recombinant host cell of claim 6 , whereinthe least one exogenous gene selected from the group consisting of an exogenous an acyl-CoA reductase gene, an exogenous alcohol dehydrogenase gene and an exogenous fatty alcohol forming acyl-CoA reductase gene is: an exogenous an acyl-CoA reductase gene.8. A method for producing a fatty alcohol claim 6 , the method comprising:culturing, in the presence of a carbon source, a recombinant host cell, 'the recombinant host cell comprises: at least one gene exogenous ...

USE OF THE REDUCTIVE GLYCINE PATHWAY FOR GENERATING FORMATOTROPHIC AND AUTOTROPHIC MICROORGANISMS

An isolated microorganism that expresses enzymes of the reductive glycine pathway is disclosed. The microorganism is capable of converting formate to pyruvate or glycerate via the formation of glycine and serine. Methods of generating same are further described. 1. An isolated microoranism that is genetically modifed to express at least one enzyme of the reductive glycine pathway , said microorganism being able to utilize formate as its sole carbon source , wherein the microorganism is capable of converting formate to glycine and serine and further being able of converting said glycine and said serine to pyruvate or glycerate.2. An isolated microorganism that is genetically modifed to express enzymes of the reductive glycine pathway , wherein the microorganism is capable of converting formate to a metabolite of central metabolism via the formation of glycine and without the formation of serine , said metabolite being selected from the group consisting of acetyl CoA , oxaloacetate , glycerate 2-phosphate and glycerate 3-phosphate.3. The microorganism of claim 2 , not expressing EC 2.1.2.1.4. The microorganism of claim 1 , further expressing a formate dehydrogenase which is capable of reducing carbon dioxide to formic acid.5. The microorganism of claim 1 , selected from the group consisting of a bacteria claim 1 , a yeast claim 1 , a fungi or an algae.6. The microorganism of claim 2 , selected from the group consisting of a bacteria claim 2 , a yeast claim 2 , a fungi or an algae.7Escherichia.. The microorganism of claim 5 , wherein said bacteria comprises8Escherichia. The microorganism of claim 7 , wherein said are genetically modified to express a first enzyme NAD-dependent formate dehydrogenase which is capable of oxidizing formate to carbon dioxide and a second enzyme formate-tetrahydrofolate ligase.9Escherichia. The microorganism of claim 8 , wherein said are genetically modified to further express bifunctional methenyltetrahydrofolate-cyclohydrolase-NAD- ...

MICROORGANISMS AND PROCESSES FOR PRODUCING TEREPHTHALIC ACID AND ITS SALTS

The invention provides non-naturally occurring microbial organisms having a (2-hydroxy-3-methyl-4-oxobutoxy)phosphonate (2H3M4OP) pathway, p-toluate pathway, and/or terephthalate pathway. The invention additionally provides methods of using such organisms to produce 2H3M4OP, p-toluate or terephthalate. Also provided herein are processes for isolating bio-based aromatic carboxylic acid, in particular, p-toluic acid or terephthalic acid, from a culture medium, wherein the processes involve contacting the culture medium with sufficient carbon dioxide (CO) to lower the pH of the culture medium to produce a precipitate comprised of the aromatic carboxylic acid. 1. A non-naturally occurring microbial organism , said microbial organism having a (2-hydroxy-3-methyl-4-oxobutoxy)phosphonate (2H3M4OP) pathway a p-toluate pathway and a terephthalate pathway and comprising at least one exogenous nucleic acid encoding a 2H3M4OP pathway enzyme expressed in a sufficient amount to produce 2H3M4OP , wherein said 2H3M4OP pathway comprises a pathway selected from:(1) 1A, 1B, 1C, 1D, 1E and 1F;(2) 2A, 2B and 2C; and(3) 2D, 2E and 2C,wherein 1A is an erythrose-4-phosphate dehydrogenase, wherein 1B is a 4-phosphoerythronate dehydrogenase, wherein 1C is a 2-acetyl-2,3-dihydroxy-4-phosphobutanoate synthase, wherein 1D is a 2-acetyl-2,3-dihydroxy-4-phosphobutanoate reductoisomerase, wherein 1E is a 2,3,4-trihydroxy-3-methyl-5-phosphopentanoate dehydratase, wherein 1F is a 4-hydroxy-3-methyl-2-oxo-5-phosphopentanoate decarboxylase, wherein 2A is a 4,5-dihydroxy-2-oxopentanoate methyltransferase, wherein 2B is a 4,5-dihydroxy-3-methyl-2-oxopentanoate kinase, wherein 2C is a 4-hydroxy-3-methyl-2-oxo-5-phosphopentanoate decarboxylase, wherein 2D is a 4,5-dihydroxy-2-oxopentanoate kinase, wherein 2E is a 4-hydroxy-2-oxo-5-phosphopentanoate methyltransferase,wherein said p-toluate pathway comprises at least one exogenous nucleic acid encoding a p-toluate pathway enzyme expressed in a sufficient ...

MICROBIAL PRODUCTION OF FATTY AMINES

The disclosure relates to recombinant microorganisms for the production of fatty amines and derivatives thereof. Further contemplated are cultured recombinant host cells as well as methods of producing fatty amines by employing these host cells. 143.-. (canceled)44. A recombinant bacterial cell for production of a fatty amine , comprising:(i) one or more expressed genes that encode an exogenous biosynthetic enzyme having thioesterase activity;(i) one or more expressed genes that encode an exogenous biosynthetic enzyme having carboxylic acid reductase activity; and(ii) one or more expressed genes that encode an exogenous biosynthetic enzyme having aminotransferase or amine dehydrogenase activity, wherein said recombinant bacterial cell produces the fatty amine in vivo.45. The recombinant bacterial cell of claim 44 , wherein said exogenous biosynthetic enzyme having thioesterase activity converts an acyl-ACP or acyl-CoA to a fatty acid.46. The recombinant bacterial cell of claim 45 , wherein said exogenous biosynthetic enzyme having carboxylic acid reductase activity converts said fatty acid to a fatty aldehyde.47. The recombinant bacterial cell of claim 46 , wherein said exogenous biosynthetic enzyme having aminotransferase or amine dehydrogenase activity converts said fatty aldehyde to a fatty amine.48. The recombinant bacterial cell of claim 44 , wherein said exogenous biosynthetic enzyme having thioesterase activity is encoded by a nucleic acid sequence that codes for a tesA gene.49. The recombinant bacterial cell of claim 44 , wherein said exogenous biosynthetic enzyme having carboxylic acid reductase activity is encoded by a nucleic acid sequence that codes for a carB gene.50. The recombinant bacterial cell of claim 44 , wherein said exogenous biosynthetic enzyme having aminotransferase activity is a putrescine or GABA aminotransferase.51. The recombinant bacterial cell of claim 50 , wherein the putrescine aminotransferase is YgjG.52. The recombinant bacterial ...

RECOMBINANT STRAIN OF BACILLUS SUBTILIS

The invention relates to a recombinant strain of , wherein pyruvate carboxylase BalpycA, glyceraldehyde-3-phosphate ferredoxin dehydrogenase gor, isocitrate NAD dehydrogenase icd, malate quinone dehydrogenase mqo, pyruvate ferredoxin oxidoreductase porAB and nitrogenase ferritin cyh are integrated and expressed in the recombinant strain. The invention also discloses use of the recombinant strain in fermentation production of acetylglucosamine. The recombinant of the invention eliminates the central carbon metabolism overflow of the and balances the intracellular reducing force, and the fermentation yield of acetylglucosamine is greatly improved. 1Bacillus subtilis. A recombinant strain of , wherein pyruvate carboxylase BalpycA , glyceraldehyde-3-phosphate ferredoxin dehydrogenase gor , isocitrate NAD dehydrogenase icd , malate quinone dehydrogenase mqo , pyruvate ferredoxin oxidoreductase porAB and nitrogenase ferritin cyh are integrated and expressed in the recombinant strain.2Bacillus subtilis. The recombinant strain according to claim 1 , wherein the recombinant strain is obtained by using BSGNKAP2 as a starting strain.3. The recombinant strain according to claim 1 , wherein the pyruvate carboxylase BalpycA claim 1 , glyceraldehyde-3-phosphate ferredoxin dehydrogenase gor claim 1 , isocitrate NAD dehydrogenase icd claim 1 , malate quinone dehydrogenase mqo claim 1 , pyruvate ferredoxin oxidoreductase porAB and nitrogenase ferritin cyh are respectively expressed by using a strong constitutive promoter.4. The recombinant strain according to claim 3 , wherein the strong constitutive promoter is P claim 3 , P claim 3 , P claim 3 , P claim 3 , P claim 3 , P claim 3 , Por Ppromoter.5Bacillus subtilis. The recombinant strain according to any one of claim 1 , wherein the encoding gene balpycA of the pyruvate carboxylase BalpycA is shown as NCBI-Protein ID: AAS42897 claim 1 , and the encoding gene balpycA of the pyruvate carboxylase BalpycA is integrated into malS claim 1 ...

Gold Optimized CAR T-cells

Control Devices are disclosed including RNA destabilizing elements (RDE), RNA control devices, and destabilizing elements (DE) combined with Chimeric Antigen Receptors (CARs) or other transgenes in eukaryotic cells. Multicistronic vectors are also disclosed for use in engineering host eukaryotic cells with the CARs and transgenes under the control of the control devices. These control devices can be used to optimize expression of CARs in the eukaryotic cells so that, for example, effector function is optimized. CARs and transgene payloads can also be engineered into eukaryotic cells so that the transgene payload is expressed and delivered after stimulation of the CAR on the eukaryotic cell. 1. (canceled)2. (canceled)3. (canceled)4. (canceled)5. (canceled)6. (canceled)7. (canceled)8. (canceled)9. (canceled)10. (canceled)11. (canceled)12. (canceled)13. (canceled)14. (canceled)15. (canceled)16. (canceled)17. (canceled)18. (canceled)19. (canceled)20. (canceled)21. A method of controlling a transgene , comprising the steps of: obtaining a primary T-cell comprising a chimeric antigen receptor , and a heterologous nucleic acid comprising a polynucleotide encoding the transgene that is operably linked to a polynucleotide encoding a RNA degradation element , wherein the RNA degradation element is an AU rich element , wherein the heterologous nucleic acid is transcribed to make a transcript encoding the transgene operably linked to the RNA degradation element , wherein the transgene encodes a payload; exposing the primary T-cell to a ligand for the chimeric antigen receptor , wherein the ligand is an antigen found on a target cell , wherein binding of the ligand by the chimeric antigen receptor activates the primary T-cell and thereby changes a metabolic state of the primary T-cell; and expressing the transgene wherein the amount of polypeptide made from the transgene is increased after the change in metabolic state of the primary T-cell.22. The method of wherein the payload ...

RECOMBINANT MICROORGANISM FOR IMPROVED PRODUCTION OF ALANINE

The present invention relates to a recombinant nucleic acid molecule, a recombinant micro-organism, to a method for producing alanine and to the use of the recombinant nucleic acid molecule or the recombinant microorganism for the fermentative production of alanine. 1. A recombinant microorganism having a higher yield and/or productivity of alanine in a fermentative production compared to a respective control microorganism , the recombinant microorganism comprising:(A) a reduced, repressed or deleted activity and/or expression of an asd gene encoding an aspartate-beta semialdehyde dehydrogenase, and (a) a reduced, repressed or deleted activity and/or expression of a pflB gene encoding a pyruvate formate lyase I,', '(b) a reduced, repressed or deleted activity and/or expression of an adhE gene encoding a bifunctional acetaldehyde-CoA dehydrogenase/iron-dependent alcohol dehydrogenase/pyruvate-formate lyase deactivase,', '(c) a reduced, repressed or deleted activity and/or expression of a ldhA gene encoding a NAO-dependent fermentative D-lactate dehydrogenase,', '(d) a reduced, repressed or deleted activity and/or expression of a pta gene encoding a phosphate acetyltransferase and/or a reduced, repressed or deleted activity and/or expression of an ackA gene encoding an acetate kinase A and propionate kinase 2,', '(e) a reduced, repressed or deleted activity and/or expression of a frdA gene encoding a fumarate reductase,', '(f) an introduced, increased or enhanced activity and/or expression of an alaD gene encoding an alanine dehydrogenase, and/or', '(g) a reduced, repressed or deleted activity and/or expression of a dadX gene encoding an alanine racemase,, '(B) at least two of the features selected from the group of'}wherein the reduction, repression, deletion, introduction, increase or enhancement of the activity and/or expression of a gene is determined compared to a respective reference microorganism.244-. (canceled)45. The recombinant microorganism of claim 1 , ...

Recombinant yeast strain for producing nervonic acids and application thereof

The present invention discloses an engineering yeast strain for producing nervonic acids. The yeast strain over-expresses the genes related to enzymes required in a synthetic process of long-chain unsaturated fatty acids, such as fatty acid elongase, desaturase, diacylglycerol acyltransferase and the like, and optionally, further adjusts and controls the synthesis and decomposition route of triglyceride, the synthesis and decomposition route of sphingomyelin, and the synthesis and decomposition route and the oxidation-reduction balanced route of lipid subcell levels. The recombinant yeast strain can produce microorganism oil; and the content of the prepared nervonic acids accounts for 39.6% of the total fatty acids.

RECOMBINANT MICROORGANISM FOR IMPROVED PRODUCTION OF ALANINE

The present invention relates to a recombinant nucleic acid molecule, a recombinant microorganism, to a method for producing alanine and to the use of the recombinant nucleic acid molecule or the recombinant microorganism for the fermentative production of alanine. 1. A recombinant microorganism comprising a reduced , repressed or deleted activity and/or expression of an asd gene or a gdhA gene.2. The recombinant microorganism of further comprising at least one of the features selected from the group of(a) an introduced, increased or enhanced activity and/or expression of an alaD gene encoding an alanine dehydrogenase,(b) a reduced, repressed or deleted activity and/or expression of a pflB gene encoding a pyruvate formate lyase I,(c) a reduced, repressed or deleted activity and/or expression of an adhE gene encoding a bifunctional acetaldehyde-CoA dehydrogenase/iron-dependent alcohol dehydrogenase/pyruvate-formate lyase deactivase,(d) a reduced, repressed or deleted activity and/or expression of a ldhA gene encoding a NAO-dependent fermentative D-lactate dehydrogenase,(e) a reduced, repressed or deleted activity and/or expression of a pta gene encoding a phosphate acetyltransferase and/or a reduced, repressed or deleted activity and/or expression of an ackA gene encoding an acetate kinase A and propionate kinase 2,(f) a reduced, repressed or deleted activity and/or expression of a frdA gene encoding a fumarate reductase, and/or 'wherein the reduction, repression, deletion, introduction, increase or enhancement of the activity and/or expression of a gene is determined compared to a respective reference microorganism.', '(g) a reduced, repressed or deleted activity and/or expression of a dadX gene encoding an alanine racemase,'}38-. (canceled)9. The recombinant microorganism of claim 1 , further comprising at least one feature selected from the group of:(a) a reduced, repressed or deleted activity and/or expression of a brnQ gene encoding a brnQ protein having a ...

METHOD FOR PRODUCING OXALATE OXIDASES HAVING ACTIVITY OPTIMUM NEAR PHYSIOLOGICAL PH AND USE OF SUCH RECOMBINANT OXALATE OXIDASES IN THE TREATMENT OF OXALATE-RELATED DISEASES

Novel oxalate oxidases are provided, which have suitable oxalate degrading activity near physiological pH (7.4). The properties of these OxOx make them potential drug candidates for use in reducing oxalate concentration in patients suffering from excess of oxalate. Especially due to the high activity at physiological pH, the OxOx's are suitable drug candidates for parenteral administration, i.e. to reduce the oxalate concentration in the plasma. 1. A recombinant oxalate oxidase having at least 60% sequence identity to the polypeptides of SEQ ID NO: 2 , SEQ ID NO: 4 ,or SEQ ID NO: 6 , or at least 99% sequence identity to the polypeptide of SEQ ID NO: 8.2. A recombinant oxalate oxidase according to having at least 70% at least 75% at least 80% claim 1 , at least 85% claim 1 , least 90% claim 1 , at least 95% claim 1 , at least 98% claim 1 , at least 99% or at least 100% sequence identity to the polypeptides of SEQ ID NO: 2 claim 1 , SEQ ID NO: 4 claim 1 , or SEQ ID NO: 6 claim 1 , or at least 100% sequence identity to the polypeptide of SEQ ID NO: 8.3. A recombinant oxalate oxidase having a relative activity of at least 20% at pH 7.5.4. A recombinant oxalate oxidase according to having a relative activity of at least 60%.5. A recombinant oxalate oxidase according to or having a relative activity of at least 80%.6. A recombinant oxalate oxidase according to any of the preceding claims having at least 60% sequence identity to the polypeptides of SEQ ID NO: 2 claim 3 , SEQ ID NO: 4 claim 3 , or SEQ ID NO: 6 claim 3 , or at least 99% sequence identity to the polypeptide of SEQ ID NO: 8.7. A recombinant oxalate oxidase according to any of the preceding claims having at least 70% at least 75% at least 80% claim 3 , at least 85% claim 3 , least 90% claim 3 , at least 95% claim 3 , at least 98% claim 3 , at least 99% or at least 100% sequence identity to the polypeptides of SEQ ID NO: 2 claim 3 , SEQ ID NO: 4 claim 3 , or SEQ ID NO: 6 claim 3 , or at least 100% sequence ...

REGULATABLE PROMOTER

A method of producing a protein of interest (POI) by culturing a recombinant eukaryotic cell line comprising an expression construct comprising a regulatable promoter and a nucleic acid molecule encoding a POI under the transcriptional control of said promoter, comprising the steps a) cultivating the cell line with a basal carbon source repressing the promoter, b) cultivating the cell line with a limited amount of a supplemental carbon source de-repressing the promoter to induce production of the POI at a transcription rate or at least 15% as compared to the native pGAP promoter, and c) producing and recovering the POI; and further an isolated regulatable promoter and a respective expression system. 1. A method of producing a protein of interest (POI) by culturing a recombinant eukaryotic cell line comprising an expression construct comprising a regulatable promoter and a nucleic acid molecule encoding a POI under the transcriptional control of said promoter , comprising the stepsa) cultivating the cell line with a basal carbon source repressing the promoter,b) cultivating the cell line with no or a limited amount of a supplemental carbon source de-repressing the promoter to induce production of the POI at a transcription rate of at least 15% as compared to the native pGAP promoter of the cell, andc) producing and recovering the POI.2. Method according to claim 1 , wherein the basal carbon source is selected from the group consisting of glucose claim 1 , glycerol claim 1 , ethanol claim 1 , a mixture thereof claim 1 , and complex nutrient material.3. Method according to or claim 1 , wherein the supplemental carbon source is a hexose such as glucose claim 1 , fructose claim 1 , galactose or mannose claim 1 , a disaccharide claim 1 , such as saccharose claim 1 , an alcohol claim 1 , such as glycerol or ethanol claim 1 , or a mixture thereof.4. Method according to any of to claim 1 , wherein step b) employs a feed medium that provides for no or the supplemental carbon ...

SYNTHETIC METHANOTROPHIC AND METHYLOTROPHIC MICROORGANISMS

Provided herein are non-naturally occurring microbial organisms comprising a methane-oxidizing metabolic pathway. The invention additionally comprises non-naturally occurring microbial organisms comprising pathways for the production of chemicals. The invention additionally provides methods for using said organisms for the production of chemicals. 1. A synthetic microorganism , wherein said synthetic microorganism comprises a natural methanol-consuming microorganism and one or more genetic modifications that improve the production of a chemical.2. (canceled)3. A synthetic microorganism comprising a natural non-methanol-consuming microorganism and one or more genetic modifications that allow said synthetic microorganism to oxidize methanol.4Escherichia coli, Bacillus subtilis, Pseudomonas putida, Saccharomyces cerevisiae, Corynebacterium glutamicum Klebsiella oxytoca, Anaerobiospirillum succiniciproducens, Actinobacillus succinogenes, Mannheimia succiniciproducens, Rhizobium etli, Gluconobacter oxydans, Zymomonas mobilis, Lactococcus lactis, Lactobacillus plantarum, Streptomyces coelicolor, Clostridium acetobutylicum, Pseudomonas fluorescens, Schizosaccharomyces pombe, Kluyveromyces lactis, Kluyveromyces marxianus, Aspergillus terreusAspergillus niger.. The synthetic microorganism of claim 3 , wherein the natural non-methanol-consuming microorganism is selected from the group consisting of claim 3 , and5Corynebacterium glutamicumEscherichia coli.. The synthetic microorganism of claim 4 , wherein the natural non-methanol-consuming microorganism is not or6. The synthetic microorganism of claim 3 , further comprising exogenous polynucleotides claim 3 , wherein said exogenous polynucleotides encode enzymes selected from the group consisting of methanol dehydrogenase (EC 1.1.1.224 or 1.1.99.37 or 1.1.2.7) claim 3 , alcohol dehydrogenase (EC 1.1.1.1) claim 3 , 3-hexulose-6-phosphate synthase (EC 4.1.2.43) and 6-phospho-3-hexuloisomerase (EC 5.3.1.27).7. The synthetic ...

MICROORGANISMS FOR THE PRODUCTION OF INSECT PHEROMONES AND RELATED COMPOUNDS

The present application relates to recombinant microorganisms useful in the biosynthesis of unsaturated C-Cfatty alcohols, aldehydes, and acetates which may be useful as insect pheromones, fragrances, flavors, and polymer intermediates. The C-Cfatty alcohols, aldehydes, and acetates described herein may be used as substrates for metathesis reactions to expand the repertoire of target compounds and pheromones. The application further relates to recombinant microorganisms co-expressing a pheromone pathway and a pathway for the production of a toxic protein, peptide, oligonucleotide, or small molecule suitable for use in an attract-and-kill pest control approach. Also provided are methods of producing unsaturated C-Cfatty alcohols, aldehydes, and acetates using the recombinant microorganisms, as well as compositions comprising the recombinant microorganisms and/or optionally one or more of the product alcohols, aldehydes, or acetates. 2Helicoverpa. The method of claim 1 , wherein the fatty acyl desaturase is a Z11 desaturase.3. The method of claim 1 , wherein the mono- or poly-unsaturated C6-C24 fatty acyl-CoA is selected from the group consisting of Z11-13:Acyl-CoA claim 1 , E11-13:Acyl-CoA claim 1 , (Z claim 1 ,Z)-7 claim 1 ,11-13:Acyl-CoA claim 1 , Z11-14:Acyl-CoA claim 1 , E11-14:Acyl-CoA claim 1 , (E claim 1 ,E)-9 claim 1 ,11-14:Acyl-CoA claim 1 , (E claim 1 ,Z)-9 claim 1 ,11-14:Acyl-CoA claim 1 , (Z claim 1 ,E)-9 claim 1 ,11-14:Acyl-CoA claim 1 , (Z claim 1 ,Z)-9 claim 1 ,11-14:Acyl-CoA claim 1 , (E claim 1 ,Z)-9 claim 1 ,11-15:Acyl-CoA claim 1 , (Z claim 1 ,Z)-9 claim 1 ,11-15:Acyl-CoA claim 1 , Z11-16:Acyl-CoA claim 1 , E11-16:Acyl-CoA claim 1 , (E claim 1 ,Z)-6 claim 1 ,11-16:Acyl-CoA claim 1 , (E claim 1 ,Z)-7 claim 1 ,11-16:Acyl-CoA claim 1 , (E claim 1 ,Z)-8 claim 1 ,11-16:Acyl-CoA claim 1 , (E claim 1 ,E)-9 claim 1 ,11-16:Acyl-CoA claim 1 , (E claim 1 ,Z)-9 claim 1 ,11-16:Acyl-CoA claim 1 , (Z claim 1 ,E)-9 claim 1 ,11-16:Acyl-CoA claim 1 , (Z claim 1 ,Z)- ...

Electrochemical Bioreactor Module and Engineered Metabolic Pathways for 1-Butanol Production with High Carbon Efficiency

A combination of an electrochemical device for delivering reducing equivalents to a cell, and engineered metabolic pathways within the cell capable of utilizing the electrochemically provided reducing equivalents is disclosed. Such a combination allows the production of commodity chemicals by fermentation to proceed with increased carbon efficiency. 1. A system for 1-butanol production , comprising:an electrochemical bioreactor module for providing reducing equivalents;a first engineered pathway for producing 1-butanol from acetyl-CoA; anda second engineered pathway for recovering carbon as formate from pyruvate, and converting the recovered formate to fructose-6-phosphate;wherein the reducing equivalents are provided to one or more redox enzymes in the first and/or second engineered pathways; and wherein optionally the first and second engineered pathways are present in an engineered cell.2. The system of wherein the first engineered pathway comprises acetyl-CoA acetyltransferase (AtoB claim 1 , EC 2.3.1.9) claim 1 , 3-hydroxybutyryl-CoA dehydrogenase (Hbd claim 1 , EC 1.1.1.157) claim 1 , 3-hydroxybutyryl-CoA dehydratase (Crt claim 1 , EC 4.2.1.5) claim 1 , trans-enoyl-CoA reductase (Ter claim 1 , EC 1.3.1.38) and aldehyde/alcohol dehydrogenase (AdhE2 claim 1 , EC 1.2.157/EC 1.1.1.1).3. The system of or wherein the second engineered pathway comprises pyruvate:formate lyase (Pfl claim 1 , EC 2.3.1.54) claim 1 , formaldehyde dehydrogenase (Fld claim 1 , EC 1.2.1.46) claim 1 , hexulose-6-phosphate synthase (HPS claim 1 , EC 4.1.2.43) claim 1 , and 6-phospho-3-hexuloisomerase (HPI claim 1 , EC 5.3.1.27).4. The system of or wherein in the engineered cell claim 1 , the endogenous pyruvate dehydrogenase (Pdh claim 1 , EC 1.2.4.1) has been disabled claim 1 , deleted or otherwise rendered non-functional.5. The system of or wherein in the engineered cell claim 1 , the endogenous fumarate reductase (FrdBC claim 1 , EC 1.3.1.6) claim 1 , lactate dehydrogenase (Ldh claim 1 , ...

MICROBIAL CONVERSION OF OILS AND FATS TO LIPID-DERIVED HIGH-VALUE PRODUCTS

A method of directly microbially converting a plant oil, an animal fat, free fatty acid, or a combination thereof to wax esters includes growing a yeast or bacterial strain in a medium comprising the plant oil, the animal fat, the free fatty acid, or combination thereof, under conditions suitable to produce the wax esters, wherein the yeast or bacterial strain is engineered to express a FAR gene encoding fatty acid alcohol reductase and a WS gene encoding a wax ester synthase, and optionally isolating the produced wax esters. Similar methods of directly microbially converting a plant oil, an animal fat, free fatty acid, or a combination thereof to omega-3 fatty acids by growing a microorganism in a medium comprising the plant oil, the animal fat, the free fatty acid, or combination thereof, under conditions suitable to produce omega-3 fatty acids are also described. 1. A method of directly microbially converting a plant oil , an animal fat , free fatty acid , or a combination thereof to wax esters , comprisinggrowing a bacterial strain in a medium comprising the plant oil, the animal fat, or a combination thereof, under conditions suitable to produce the wax esters, wherein the bacterial strain is engineered to express a FAR gene encoding fatty acid alcohol reductase and a WS gene encoding a wax ester synthase,orgrowing a yeast strain in a medium comprising the plant oil, the animal fat, the free fatty acid, or a combination thereof, under conditions suitable to produce the wax esters, wherein the yeast strain is engineered to express a FAR gene encoding fatty acid alcohol reductase and a WS gene encoding a wax ester synthase, andoptionally isolating the produced wax esters.2. The method of claim 1 , wherein the microbe is a bacterial or yeast strain and the medium is glucose-free.3. The method of claim 1 , wherein the plant oil comprises palm oil claim 1 , soybean oil claim 1 , corn oil claim 1 , rapeseed oil claim 1 , peanut oil claim 1 , sunflower oil claim 1 , ...

BENZYLISOQUINOLINE ALKALOID (BIA) PRECURSOR PRODUCING MICROBES, AND METHODS OF MAKING AND USING THE SAME

Host cells that are engineered to produce benzylisoquinoline alkaloid (BIAs) precursors, such as norcoclaurine (NC) and norlaudanosoline (NL), are provided. The host cells may have one or more engineered modifications selected from: a feedback inhibition alleviating mutation in a enzyme gene; a transcriptional modulation modification of a biosynthetic enzyme gene, an inactivating mutation in an enzyme; and a heterologous coding sequence. Also provided are methods of producing a BIA of interest or a precursor thereof using the host cells and compositions, e.g., kits, systems etc., that find use in methods of the invention. 114.-. (canceled)15. An engineered non-plant cell comprising coding sequence modifications with a feedstock , wherein the coding sequence modifications comprise a heterologous coding sequence that encodes an enzyme , a feedback inhibition alleviating mutation in enzyme genes and an inactivating mutation in enzymes , and the enzymes participate in the metabolic pathway producing the benzylisoquinoline alkaloid precursor product ,wherein the benzylisoquinoline alkaloid precursor product is selected from the group consisting of 4-hydroxyphenylacetaldehyde, 4-hydroxyphenylpyruvic acid, L-3,4-dihydroxyphenylalanine, 3,4-dihydroxyphenylacetaldehyde, dopamine, norcoclaurine and norlaudanosoline,wherein the heterologous coding sequence encodes one or more enzymes selected from the group consisting of TYR, TyrH, FOL2, PTPS, SepR, PCD, QDHPR, DODC, TYDC, MAO, NCS, 6OMT, CNMT and 4′OMT;wherein the feedback inhibition alleviating mutation in enzyme genes affects one or more enzymes selected from the group consisting of ARO4 and ARO7; andwherein the inactivating mutation in enzymes involves inactivation of one or more enzymes selected from the group consisting of ZWF1, ADH2, ADH5, ADH6, ALD2, ALD3, ALD4, ALD5 and ALD6.16. The engineered non-plant cell according to claim 15 , wherein the coding sequence modifications further comprise a transcriptional modulation ...

Engineered CO2-Fixing Chemotrophic Microorganisms Producing Carbon-Based Products and Methods of Using the Same

Disclosed herein are microorganisms containing exogenous or heterologous nucleic acid sequences, wherein the microorganisms are capable of growing on gaseous carbon dioxide, gaseous hydrogen, syngas, or combinations thereof. In some embodiments the microorganisms are chemotrophic bacteria that produce or secrete at least 10% of lipid by weight. Also disclosed are methods of fixing gaseous carbon into organic carbon molecules useful for industrial processes. Also disclosed are methods of manufacturing chemicals or producing precursors to chemicals useful in jet fuel, diesel fuel, and biodiesel fuel. Exemplary chemicals or precursors to chemicals useful in fuel production are alkanes, alkenes, alkynes, fatty acid alcohols, fatty acid aldehydes, desaturated hydrocarbons, unsaturated fatty acids, hydroxyl acids, or diacids with carbon chains between six and thirty carbon atoms long. Also disclosed are microorganisms and methods using disclosed microorganisms for the production of butanediol and its chemical precursors in low-oxygen or anaerobic fermentation. Also disclosed are microorganisms and methods using disclosed microorganisms for generating hydroxylated fatty acids in microbes through the transfer of enzymes that are known to hydroxylate fatty acids in plants or microbes. Also disclosed are microorganisms and methods using disclosed microorganisms for the production of shorter-chain fatty acids in microbes through the introduction of exogenous fatty acyl-CoA binding proteins. 1Cupriavidus, Xanthobacter, HydrogenobacterHydrogenovibrio. A bacterial cell of the genus , or comprising at least a first exogenous nucleic acid sequence , wherein the cell converts gaseous COand/or gaseous Hand/or syngas into one or more lipids or hydrocarbons.299.-. (canceled)100. The bacterial cell of claim 1 , wherein the first exogenous nucleic acid sequence encodes a fatty acyl-CoA binding protein.101. The bacterial cell of claim 100 , further comprising a second exogenous nucleic ...

ALDEHYDE DEHYDROGENASE VARIANTS AND METHODS OF USE

The invention provides polypeptides and encoding nucleic acids of aldehyde dehydrogenase variants. The invention also provides cells expressing aldehyde dehydrogenase variants. The invention further provides methods for producing 3-hydroxybutyraldehyde (3-HBal) and/or 1,3-butanediol (1,3-BDO), or an ester or amide thereof, comprising culturing cells expressing an aldehyde dehydrogenase variant or using lysates of such cells. The invention additional provides methods for producing 4-hydroxybutyraldehyde (4-HBal) and/or 1,4-butanediol (1,4-BDO), or an ester or amide thereof, comprising culturing cells expressing an aldehyde dehydrogenase variant or using lysates of such cells. 1. An isolated nucleic acid molecule selected from:(a) a nucleic acid molecule encoding an amino acid sequence referenced as SEQ ID NO:1, 2 or 3 or in Table 4, wherein said amino acid sequence comprises one or more of the amino acid substitutions set forth in Table 1, 2 and/or 3;(b) a nucleic acid molecule that hybridizes to the nucleic acid of (a) under highly stringent hybridization conditions and comprises a nucleic acid sequence that encodes one or more of the amino acid substitutions set forth in Table 1, 2 and/or 3;(c) a nucleic acid molecule encoding an amino acid sequence comprising the consensus sequence of Loop A (SEQ ID NO:5) and/or Loop B (SEQ ID NO:6), wherein said amino acid sequence comprises one or more of the amino acid substitutions set forth in Table 1, 2 and/or 3; and(d) a nucleic acid molecule that is complementary to (a) or (b).2. The isolated nucleic acid molecule of claim 1 , wherein said amino acid sequence claim 1 , other than the one or more amino acid substitutions claim 1 , has at least 65% claim 1 , 70% claim 1 , 75% claim 1 , 80% claim 1 , 85% claim 1 , 90% claim 1 , 95% claim 1 , 98% or 99% sequence identity claim 1 , or is identical claim 1 , to an amino acid sequence referenced in SEQ ID NO:1 claim 1 , 2 or 3 or in Table 4.3. The nucleic acid of or claim 1 , ...

HIGH YIELD ROUTE FOR THE PRODUCTION OF COMPOUNDS FROM RENEWABLE SOURCES

Provided herein are methods, compositions, and non-naturally occurring microbial organism for preparing compounds such as 1-butanol, butyric acid, succinic acid, 1,4-butanediol, 1-pentanol, pentanoic acid, glutaric acid, 1,5-pentanediol, 1-hexanol, hexanoic acid, adipic acid, 1,6-hexanediol, 6-hydroxy hexanoic acid, ε-Caprolactone, 6-amino-hexanoic acid, ε-Caprolactam, hexamethylenediamine, linear fatty acids and linear fatty alcohols that are between 7-25 carbons long, linear alkanes and linear α-alkenes that are between 6-24 carbons long, sebacic acid and dodecanedioic acid comprising: a) converting a Caldehyde and pyruvate to a Cβ-hydroxyketone intermediate through an aldol addition; and b) converting the Cβ-hydroxyketone intermediate to the compounds through enzymatic steps, or a combination of enzymatic and chemical steps. 1. A non-naturally occurring microbial organism comprising at least one exogenous nucleic acid encoding a 1 ,6-hexanediol pathway enzyme.2. The microbial organism of further comprising at least one enzyme selected from 2A wherein 2A is a 4-hydroxy-2-oxo-adipate aldolase claim 1 , or a 4 claim 1 ,6-dihydroxy-2-oxo-hexanoate aldolase.327-. (canceled)28. A non-naturally occurring microbial organism claim 1 , comprising at least one exogenous nucleic acid encoding a 1 claim 1 ,6-hexanediol pathway enzyme selected from 2A and one or more of 2B claim 1 , 3B1 claim 1 , 3B2 claim 1 , wherein 2A is a 4-hydroxy-2-oxo-adipate aldolase or a 4 claim 1 ,6-dihydroxy-2-oxo-hexanoate aldolase claim 1 , 2B is a 4-hydroxy-2-oxo-adipate dehydratase or a 4 claim 1 ,6-dihydroxy-2-oxo-hexanoate 4-dehydratase claim 1 , 3B1 is a 4-hydroxy-2-oxo-adipate 2-reductase or a 4 claim 1 ,6-dihydroxy-2-oxo-hexanoate 2-reductase claim 1 , and 3B2 is a 4-hydroxy-2-oxo-adipate 4-dehydrogenase or a 4 claim 1 ,6-dihydroxy-2-oxo-hexanoate 4-dehydrogenase.29. The organism of claim 28 , further comprising a 1 claim 28 ,6-hexanediol pathway enzyme selected from one or more of 2C claim ...

Polypeptides with Ketol-Acid Reductoisomerase Activity

Polypeptides having ketol-acid reductoisomerase activity are provided. Also disclosed are recombinant host cells comprising isobutanol biosynthetic pathways employing such polypeptides. Methods for producing isobutanol employing host cells comprising the polypeptides having ketol-acid reductoisomerase activity are also disclosed. 1. A recombinant host cell comprising an isobutanol biosynthetic pathway anda. a heterologous polypeptide with ketol-acid reductoisomerase activity having at least about 85%, at least about 90% identity, at least about 95%, or at least about 98% identity to one of the following: K9JM2 (SEQ ID NO: 193), K9JM3 (SEQ ID NO: 194), K9JM4 (SEQ ID NO: 195), K9JM5 (SEQ ID NO: 196), K9JM6 (SEQ ID NO: 197), K9JM7 (SEQ ID NO: 198), K9JM8 (SEQ ID NO: 199), K9JM9 (SEQ ID NO: 200), K9JM10 (SEQ ID NO: 201), K9JM11 (SEQ ID NO: 202), K9JM12 (SEQ ID NO: 203), K9JM13 (SEQ ID NO: 204), K9JM14 (SEQ ID NO: 205), K9JM15 (SEQ ID NO: 206), K9JM16 (SEQ ID NO: 207), K9JM17 (SEQ ID NO: 208), K9JM18 (SEQ ID NO: 209), K9JM19 (SEQ ID NO: 210), K9JM20 (SEQ ID NO: 211), K9JM21 (SEQ ID NO: 212), K9JM22 (SEQ ID NO: 213), K9JM23 (SEQ ID NO: 214), K9JM24 (SEQ ID NO: 215), K9JM25 (SEQ ID NO: 216), K9JM26 (SEQ ID NO: 217), K9JM27 (SEQ ID NO: 218), K9JM28 (SEQ ID NO: 219), K9JM29 (SEQ ID NO: 220), K9JM30 (SEQ ID NO: 221), K9JM31 (SEQ ID NO: 222), JM32 (SEQ ID NO: 223), JM33 (SEQ ID NO: 224), JM34 (SEQ ID NO: 225), JM35 (SEQ ID NO: 226), JM36 (SEQ ID NO: 227), JM37 (SEQ ID NO: 228), JM38 (SEQ ID NO: 229), JM39 (SEQ ID NO: 230), JM40 (SEQ ID NO: 231), JM42 (SEQ ID NO: 232), JM43 (SEQ ID NO: 233), JM44 (SEQ ID NO: 234), K9SB2 (SEQ ID NO: 235), K9_DAVID_SH (SEQ ID NO: 236), K9ALL3 (SEQ ID NO: 237), K9_URSALA (K9SB2+A56V) (SEQ ID NO: 239), JM41 (SEQ ID NO: 240), K9ALL148 (SEQ ID NO: 241), K9JM148 (SEQ ID NO: 242), K9ALL156 (SEQ ID NO: 243), K9JM156 (SEQ ID NO: 244), K9ALL191 (SEQ ID NO: 245), K9JM191 (SEQ ID NO: 246), K9ALL254 (SEQ ID NO: 247), K9ALL278 (SEQ ID NO: 248), K9ALL37 (SEQ ...

Micro-organism and Methods of Use

The invention relates to a micro-organism comprising a hydrogenase enzyme system which is capable of converting carbon dioxide into formic acid and a second enzyme system which is capable of converting formic acid into aliphatic carboxylic acids having a chain length of five or more carbon atoms. Also described are various methods for producing oil, as well as other aspects of the invention. 1. A method of producing formic acid , comprising.{'i': 'Acetobacter', 'claim-text': {'br': None, 'sub': 2', '2, 'CO+H→HCOOH.'}, 'contacting a culture medium comprising a micro-organism consisting of the strain having accession number NCIMB 41808, or a micro-organism derived therefrom, with carbon dioxide under conditions permitting reduction of the carbon dioxide to formic acid2. The method of claim 1 , wherein the micro-organism is present in the culture medium at 20%.3. The method of claim 1 , further comprisingintroducing a disinfectant or antimicrobial agent into the culture medium to kill the micro-organism.4. The method of claim 3 , wherein the micro-organism is killed prior to contacting the culture medium with CO2.5. The method of claim 1 , wherein the culture medium comprises a minimal medium.6. The method of claim 1 , wherein carbon dioxide is the sole source of carbon.7. The method of claim 6 , wherein carbon dioxide is bubbled through the medium.8. The method of claim 1 , wherein the conditions comprise a pH of between about 3.0 and about 8.5.9. The method of wherein the conditions comprise a pH between about 6.0 and about 7.0.10. The method of claim 1 , wherein the conditions comprise a temperature of between about 5° C. and about 60° C.11. The method of claim 10 , wherein the conditions comprise a temperature of between about 15° C. and about 20° C.12. The method of claim 1 , wherein the medium comprises a carbon dioxide sequestering agent.13. The method of claim 1 , wherein the medium comprises an oxidising agent.14. The method of claim 1 , wherein the culture ...

ANAEROBIC FERMENTATIVE PRODUCTION OF FURANDICARBOXYLIC ACID

The present disclosure provides recombinant microorganisms and methods for the anaerobic production of 2,4-furandicarboxylic acid from one or more carbon sources. The microorganisms and methods provide redox-balanced and ATP positive pathways for co-producing 2,4-furandicarboxylic acid with ethanol and for co-producing 2,4-furandicarboxylic acid with ethanol and 1-propanol. The method provides recombinant microorganisms that express endogenous and/or exogenous nucleic acid molecules encoding polypeptides that catalyze the conversion of a carbon source into 2,4-furandicarboxylic acid and that coupled the 2,4-furandicarboxylic acid pathway with an additional metabolic pathway.

Biosynthetic methods and systems for producing monosaccharides

The present disclosure is related to biosynthetic methods of forming monosaccharides, and systems for generating the same. A benefit of the methods and systems disclosed herein can include the sustainable production of monosaccharides in an automated process. A benefit of the methods and systems herein can be the generation of monosaccharides from renewable source materials. An additional benefit of the methods and systems herein can include the use of abundant feedstocks, such as carbon dioxide, for the efficient generation of select monosaccharides for use as nutrients and for other useful applications. Another benefit of the methods and systems disclosed herein can include reduction of excess carbon dioxide from the environment.

FUNCTIONALIZED NANOPARTICLES FOR ENHANCED AFFINITY PRECIPITATION OF PROTEINS

The present invention provides a nanoparticle capable of binding specifically to a target protein in a solution and precipitating with the target protein out of the solution upon addition of the target protein to the solution. The precipitation may be reversed release the target protein from the nanoparticle, which may be reused for precipitating the target protein. Also provided are a method for purifying a target protein by affinity precipitation using the nanoparticle without chromatography and a method for preparing the nanoparticle. 1. A nanoparticle comprising a fusion protein and a scaffolding domain , wherein the fusion protein is covalently bound to the scaffolding domain , wherein the fusion protein comprises an affinity domain specific for a target protein and a stimuli responsive precipitation domain , wherein the scaffolding domain comprises self-assembled proteins and has a diameter of at least 10 nm , wherein the nanoparticle is soluble in a first solution in the absence of the target protein , wherein the nanoparticle is capable of binding specifically to the target protein in the first solution and precipitating with the target protein out of the first solution in response to a first stimulus , and wherein the first stimulus comprises addition of the target protein to the first solution.2. The nanoparticle of claim 1 , wherein the precipitated nanoparticle is capable of being solubilized in a second solution to release the target protein from the nanoparticle in the second solution in response to a second stimulus.3. The nanoparticle of claim 1 , wherein the first stimulus consists of addition of the target protein to the first solution claim 1 , wherein the first solution has a temperature of 15-25° C. claim 1 , a salt concentration of 50-200 mM and a pH of pH 6-9 claim 1 , and wherein the molar ratio of the affinity domain to the target protein in the first solution is in the range of 3:1-6:1.4. The nanoparticle of claim 1 , wherein the first ...

Microorganisms and methods for production of specific length fatty alcohols and related compounds

The invention provides non-naturally occurring microbial organisms containing a fatty alcohol, fatty aldehyde or fatty acid pathway, wherein the microbial organisms selectively produce a fatty alcohol, fatty aldehyde or fatty acid of a specified length. Also provided are non-naturally occurring microbial organisms having a fatty alcohol, fatty aldehyde or fatty acid pathway, wherein the microbial organisms further include an acetyl-CoA pathway. In some aspects, the microbial organisms of the invention have select gene disruptions or enzyme attenuations that increase production of fatty alcohols, fatty aldehydes or fatty acids. The invention additionally provides methods of using the above microbial organisms to produce a fatty alcohol, a fatty aldehyde or a fatty acid.

A BACTERIAL CELL FACTORY FOR EFFICIENT PRODUCTION OF ETHANOL FROM WHEY

The invention relates to a method for homo-ethanol production from lactose using a genetically modified lactic acid bacterium of the invention, where the cells are provided with a substrate comprising dairy waste supplemented with an amino nitrogen source (such as acid hydrolysed corn steep liquor). The invention further relates to genetically modified lactic acid bacterium and its use for homo-ethanol production from lactose in dairy waste. The lactic acid bacterium comprises both genes (lacABCD, LacEF, lacG) encoding enzymes catalysing the lactose catabolism pathway; and transgenes (pdc and adhB) encoding enzymes catalysing the conversion of pyruvate to ethanol. Additionally a number of genes (ldh, pta and adhE) are deleted in order to maximise homo-ethanol production as compared to production of lactate, acetoin and acetate production. 1. A method for ethanol production using a genetically engineered lactic acid bacterium comprising the steps of:a. introducing a genetically modified lactic acid bacterium into an aqueous culture medium;b. incubating the culture of (a);c. recovering ethanol produced by said culture during step (b), and optionally wherein the aqueous culture medium comprises:', 'I. whey permeate or residual whey permeate, and', wherein the genetically engineered lactic acid bacterium comprises transgenes encoding:', 'i. a polypeptide having pyruvate decarboxylase (PDC) activity (EC 4.1.1.1); and', 'wherein the genome of said lactic acid bacterium comprises genes encoding polypeptides having:', 'ii. a polypeptide having alcohol dehydrogenase B activity (EC 1.1.1.1); and'}, 'iii. lactose-specific phosphotransferase system (PTS) activity (EC 2.7.1.69)', 'iv. phospho-β-D-galactosidase activity (EC 3.2.1.85)', 'v. galactose-6-phosphate isomerase activity (EC 5.3.1.26),', 'vi. D-tagatose-6-phosphate kinase activity (EC 2.7.1.114), and', 'wherein the genome of said lactic acid bacterium is deleted for genes or lacks functional genes or genes encoding ...

ORGANISMS FOR THE PRODUCTION OF 1,3-BUTANEDIOL

A non-naturally occurring microbial organism includes a microbial organism having a 1,3-butanediol (1,3-BDO) pathway having at least one exogenous nucleic acid encoding a 1,3-BDO pathway enzyme expressed in a sufficient amount to produce 1,3-BDO. The pathway includes an enzyme selected from a 2-amino-4-ketopentanoate (AKP) thiolase, an AKP dehydrogenase, a 2-amino-4-hydroxypentanoate aminotransferase, a 2-amino-4-hydroxypentanoate oxidoreductase (deaminating), a 2-oxo-4-hydroxypentanoate decarboxylase, a 3-hydroxybutyraldehyde reductase, an AKP aminotransferase, an AKP oxidoreductase (deaminating), a 2,4-dioxopentanoate decarboxylase, a 3-oxobutyraldehyde reductase (ketone reducing), a 3-oxobutyraldehyde reductase (aldehyde reducing), a 4-hydroxy-2-butanone reductase, an AKP decarboxylase, a 4-aminobutan-2-one aminotransferase, a 4-aminobutan-2-one oxidoreductase (deaminating), a 4-aminobutan-2-one ammonia-lyase, a butenone hydratase, an AKP ammonia-lyase, an acetylacrylate decarboxylase, an acetoacetyl-CoA reductase (CoA-dependent, aldehyde forming), an acetoacetyl-CoA reductase (CoA-dependent, alcohol forming), an acetoacetyl-CoA reductase (ketone reducing), a 3-hydroxybutyryl-CoA reductase (aldehyde forming), a 3-hydroxybutyryl-CoA reductase (alcohol forming), a 4-hydroxybutyryl-CoA dehydratase, and a crotonase. A method for producing 1,3-BDO, includes culturing such microbial organisms under conditions and for a sufficient period of time to produce 1,3-BDO. 1. A non-naturally occurring microbial organism , comprising a microbial organism having a 1 ,3-butanediol (1 ,3-BDO) pathway comprising at least one exogenous nucleic acid encoding a 1 ,3-BDO pathway enzyme expressed in a sufficient amount to produce 1 ,3-BDO , said 1 ,3-BDO pathway comprising an enzyme selected from the group consisting of a 2-amino-4-ketopentanoate (AKP) thiolase , an AKP dehydrogenase , a 2-amino-4-hydroxypentanoate aminotransferase , a 2-amino-4-hydroxypentanoate oxidoreductase ( ...

MICROORGANISMS FOR THE PRODUCTION OF 1,4-BUTANEDIOL

The invention provides non-naturally occurring microbial organisms comprising a 1,4-butanediol (BDO) pathway comprising at least one exogenous nucleic acid encoding a BDO pathway enzyme expressed in a sufficient amount to produce BDO. The invention additionally provides methods of using such microbial organisms to produce BDO. 139-. (canceled)40. A recombinant microorganism adapted to biosynthesize 1 ,4-butanediol (“1 ,4-BDO”) , the recombinant microorganism comprising one or more nucleic acid sequences encoding one or more of 1) a first polypeptide providing acetyl-CoA acetyltransferase activity , 2) a second polypeptide providing β-hydroxybutyryl-CoA dehydrogenase activity; 3) a third polypeptide providing crotonase activity; a 4) fourth polypeptide providing vinylacetyl-CoA-Δ-isomerase and 4-hydroxybutyryl-CoA dehydratase activities; 5) a fifth polypeptide providing 4-hydroxybutyrate-CoA-hydrolase activity , and 6) a sixth polypeptide providing 1 ,3-propanediol dehydrogenase activity , wherein the recombinant microorganism biosynthesizes 1 ,4-BDO utilizing said polypeptides.41. The recombinant microorganism of claim 40 , wherein the one or more nucleic acid sequences comprise at least one of thiL claim 40 , hbd claim 40 , crt claim 40 , abfD claim 40 , abfT claim 40 , and dhaT.42. The recombinant microorganism of claim 40 , wherein the recombinant microorganism is adapted to biosynthesize 1 claim 40 ,4-BDO by condensing two acetyl-CoA moieties into acetoacetyl-CoA.43. The recombinant microorganism of claim 42 , comprising aldehyde dehydrogenase.44. (canceled)45. A recombinant microorganism adapted to biosynthesize 1 claim 42 ,4-butanediol (“1 claim 42 ,4-BDO”) claim 42 , the recombinant microorganism comprising one or more nucleic acid sequences encoding one or more of 1) a first polypeptide providing a-ketoglutarate decarboxylase activity claim 42 , 2) a second polypeptide providing 4-hydroxybutyrate dehydrogenase activity claim 42 , and 3) a third polypeptide ...

CULTURE MODIFIED TO CONVERT METHANE OR METHANOL TO 3-HYDROXYPROPRIONATE

Provided are engineered organisms which can convert methane or methanol to 3-hydroxypropionate. 1. A synthetic culture comprising one or more microorganisms comprising one or more modifications that improve the production of a product from a substrate , wherein the substrate comprises methane and/or methanol.2. The synthetic culture according to claim 1 , wherein the substrate comprises methane.3. The synthetic culture according to claim 2 , wherein the product comprises 3-hydroxyproprionate.4. The synthetic culture according to claim 1 , wherein the product comprises 3-hydroxyproprionate.5. The synthetic culture according to claim 1 , wherein the product comprises a substance derived from acetyl-CoA and/or malonyl-CoA.6Escherichia coli.. The synthetic culture according to claim 1 , wherein at least one of the one or more microorganisms comprises7. The synthetic culture according to claim 1 , wherein the one or more microorganisms comprises a first at least one microorganism and a second at least one microorganism claim 1 , wherein the first at least one microorganism produces methanol from methane and the second at least one microorganism produces 3-hydroxypropionate from methanol.8. The synthetic culture according to claim 1 , wherein the one or more modifications comprise exogenous polynucleotides or deletion of one or more genes.9. The synthetic culture according to claim 8 , wherein the exogenous polynucleotides encode polypeptides selected from one or more polypeptides comprising methane monooxygenase (EC 1.14.13.25) claim 8 , malonyl-CoA reductase (EC 1.2.1.75) claim 8 , acetyl-CoA carboxylase (EC 6.4.1.2) claim 8 , methanol dehydrogenase (EC 1.1.1.244 or EC 1.1.2.7) claim 8 , 3-hexulose-6-phosphate synthase (EC 4.1.2.43) claim 8 , and/or 6-phospho-3-hexuloisomerase (EC 5.3.1.27).10Bacillus methanolicus, Bacillus stearothermophilusCorynebacterium glutamicum.. The synthetic culture according to claim 9 , wherein the methanol dehydrogenase comprises a methanol ...

A MICROORGANISM HAVING ENHANCED ACTIVITY OF ALPHA-KETOGLUTARATE DECARBOXYLASE AND A METHOD OF PRODUCING 1,4-BUTANEDIOL USING THE SAME

Provided are a microorganism having an enhanced activity of alpha-ketoglutarate decarboxylase and a method of producing 4-hydroxybutyrate or 1,4-butanediol using the same. 1. A recombinant microorganism having an increased activity of converting alpha-ketoglutarate to succinic semi-aldehyde , wherein the increased activity is caused by an increase in expression of alpha-ketoglutarate dehydrogenase E1 component.2EscherichiaCorynebacterium.. The recombinant microorganism of claim 1 , wherein the recombinant microorganism belongs to the genus or the genus3E. coli.. The recombinant microorganism of claim 1 , wherein the microorganism is4. The recombinant microorganism of claim 1 , wherein the increase in expression of alpha-ketoglutarate dehydrogenase E1 component is caused by an increase in expression of an endogenous polynucleotide encoding alpha-ketoglutarate dehydrogenase E1 component.5. The recombinant microorganism of claim 1 , wherein the alpha-ketoglutarate dehydrogenase E1 component comprises SEQ ID NO: 1 or 3.6. The microorganism of claim 1 , wherein the recombinant microorganism comprises an exogenous polynucleotide encoding alpha-ketoglutarate dehydrogenase E1 component.7EscherichiaCorynebacterium.. The recombinant microorganism of claim 6 , wherein the polynucleotide encoding alpha-ketoglutarate dehydrogenase E1 component is from the genus or the genus8. The recombinant microorganism of claim 6 , wherein the polynucleotide encoding alpha-ketoglutarate dehydrogenase E1 component comprises SEQ ID NO: 2 or 4.9. The recombinant microorganism of claim 1 , wherein the recombinant microorganism converts succinic semi-aldehyde to 4-hydroxybutyrate.10. The recombinant microorganism of claim 9 , wherein the recombinant microorganism expresses a polynucleotide encoding 4-hydroxybutyrate dehydrogenase claim 9 , which converts succinic semi-aldehyde to 4-hydroxybutyrate.11. The recombinant microorganism of claim 10 , wherein the 4 hydroxybutyrate dehydrogenase comprises ...

MICROORGANISM PRODUCING 4-HYDROXYBUTYRATE AND A METHOD FOR PRODUCING 4-HYDROXYBUTYRATE IN ANAEROBIC CONDITION USING THE SAME

A genetically modified microorganism comprising a polynucleotide encoding α-ketoglutarate synthase or a mutant thereof, and a polynucleotide encoding pyruvate carboxylase or a mutant thereof; wherein the genetically modified microorganism has decreased malate quinone oxidoreductase activity and/or decreased phosphoenolpyruvate carboxykinase activity compared to an unmodified microorganism of the same type, and wherein the genetically modified microorganism produces 4-hydroxybutyrate. 1. A genetically modified microorganism comprisinga polynucleotide encoding exogenous α-ketoglutarate synthase, anda polynucleotide encoding endogenous pyruvate carboxylase or a mutant thereof;wherein the genetically modified microorganism has decreased malate quinone oxidoreductase activity, decreased phosphoenolpyruvate carboxykinase activity, or a combination thereof, compared to an unmodified microorganism of the same type,and wherein the genetically modified microorganism produces 4-hydroxybutyrate.2. The genetically modified microorganism of claim 1 , wherein the microorganism comprises a polynucleotide encoding succinyl-CoA:coenzyme A transferase or a mutant thereof claim 1 , a polynucleotide encoding coenzyme A-dependent succinate semialdehyde dehydrogenase or a mutant thereof claim 1 , and a polynucleotide encoding 4-hydroxybutyrate dehydrogenase or a mutant thereof.3. The genetically modified microorganism of claim 1 , wherein the microorganism has decreased succinate semialdehyde dehydrogenase activity compared to an unmodified microorganism of the same type.4. The genetically modified microorganism of claim 1 , wherein one or more of NCgl0049 claim 1 , NCgl0463 claim 1 , and NCgl2619 genes in the microorganism has an addition claim 1 , substitution claim 1 , or deletion mutation that eliminates succinate semialdehyde dehydrogenase activity.5. The genetically modified microorganism of claim 4 , wherein the NCgl0049 gene comprises the nucleic acid sequence of SEQ ID NO: 22 ...

HYDROCARBON SYNTHASE GENE AND USE THEREOF

A hydrocarbon synthase gene encoding protein having excellent capacity to synthesize a hydrocarbon such as alkane and novel functions is provided. The gene encodes a protein comprising an amino acid sequence comprising a motif sequence shown in SEQ ID NO: 1 and having activity of synthesizing a hydrocarbon with a carbon number one less than that of an aldehyde compound from the aldehyde compound. 1. A gene encoding a protein comprising an amino acid sequence comprising a motif sequence shown in SEQ ID NO: 1 and having activity of synthesizing a hydrocarbon with a carbon number one less than that of an aldehyde compound from the aldehyde compound.2. The gene according to claim 1 , wherein the protein further comprises a motif sequence shown in SEQ ID NO: 2 on the C-terminal side of the motif sequence shown in SEQ ID NO: 1.3. The gene according to claim 1 , wherein the protein is any of the following (a) to (d):(a) a protein comprising an amino acid sequence shown in any even-numbered sequence ID number of SEQ ID NOS: 3 to 32 and 65 to 170;(b) a protein comprising an amino acid sequence derived from the amino acid sequence shown in any even-numbered sequence ID number of SEQ ID NOS: 3 to 32 and 65 to 170 by substitution, deletion, insertion, or addition of one or a plurality of amino acids and having activity of synthesizing a hydrocarbon with a carbon number one less than that of an aldehyde compound from the aldehyde compound;(c) a protein comprising an amino acid sequence having 70% or more identity to an amino acid sequence shown in any even-numbered sequence ID number of SEQ ID NOS: 3 to 32 and 65 to 170 and having activity of synthesizing a hydrocarbon with a carbon number one less than that of an aldehyde compound from the aldehyde compound; and(d) a protein encoded by a polynucleotide that hybridizes under stringent conditions to at least a portion of a polynucleotide comprising a sequence complementary to a nucleotide sequence shown in any odd-numbered ...

Control of growth-induction-production phases

The present invention provides various combinations of genetic modifications to a transformed host cell that provide increase conversion of carbon to a chemical product. The present invention also provides methods of fermentation and methods of making various chemical products.

MUTANT CYANOBACTERIA AND METHOD TO ENHANCE PHOTOSYNTHETIC GROWTH AND BIOMASS PRODUCTION OF CYANOBACTERIA

The present invention relates to a mutant cyanobacterium and a method to increase photosynthetic growth and/or biomass production of cyanobacteria by using the same. 1. A mutant cyanobacterium expressing a mutant cytochrome polypeptide selected from the group consisting of:(a) a mutant cytochrome b559 α polypeptide having an amino acid substitution with alanine (A) at a position corresponding to position 23 in a cytochrome b559 a polypeptide having SEQ ID NO: 1;(b) a mutant cytochrome b559 β polypeptide having an amino acid substitution with alanine (A) or valine (V) at a position corresponding to position 28 in a cytochrome b559 β polypeptide having SEQ ID NO: 2, or an amino acid substitution with phenylalanine (F) at a position corresponding to position 32 in a cytochrome b559 β polypeptide having SEQ ID NO: 2; and(c) a mutant cytochrome PsbJ polypeptide having an amino acid substitution with phenylalanine (F) or arginine (R) at a position corresponding to position 16 in a cytochrome PsbJ polypeptide having SEQ ID NO: 3, or an amino acid substitution with phenylalanine (F) at a position corresponding to position 20 in a cytochrome PsbJ polypeptide having SEQ ID NO: 3.2. The mutant cyanobacterium of claim 1 , which exhibits weakened effects of blue-light-induced nonphotochemical fluorescence quenching (NPQ) when compared with a wild type cyanobacteria under the same conditions.3. The mutant cyanobacterium of claim 1 , which exhibits enhanced effects of state transitions under medium blue light claim 1 , when compared with a wild type cyanobacteria under the same conditions.4. The mutant cyanobacterium of claim 1 , which exhibits increased photosynthetic growth rate and/or biomass production claim 1 , when compared with a wild type cyanobacteria under the same conditions.5. The mutant cyanobacterium of claim 1 , which expresses a normal level of an orange carotenoid protein (OCP) as in a wild type cyanobacteria under the same conditions.6. The mutant cyanobacterium ...

PYRUVATE DEHYDROGENASE VARIANTS, A MICROORGANISM COMPRISING THE SAME AND A METHOD FOR PRODUCING L-AMINO ACID USING THE SAME

The present disclosure relates to a novel pyruvate dehydrogenase variant, a polynucleotide encoding the pyruvate dehydrogenase variant, a microorganism of the genus producing L-amino acid, which includes the pyruvate dehydrogenase variant, and a method for producing an L-amino acid using the microorganism. 1. A pyruvate dehydrogenase variant comprising at least one amino acid substitutions in a region of amino acids at positions from 190 to 205 or in a region of amino acids at positions from 415 to 440 of SEQ ID NO: 1.2. The pyruvate dehydrogenase variant of claim 1 , wherein the amino acid substitution in the region of amino acids at positions from 190 to 205 of SEQ ID NO: 1 is selected from the group consisting of amino acids at positions 190 claim 1 , 195 claim 1 , 199 claim 1 , and 201.3. The pyruvate dehydrogenase variant of claim 1 , wherein the amino acid substitution in the region of amino acids at positions from 190 to 205 of SEQ ID NO: 1 is selected from the group consisting of a substitution at position 190 from glutamic acid to valine (E190V) claim 1 , a substitution at position 195 from glutamine to histidine (Q195H) claim 1 , a substitution at position 199 from proline to serine (P199S) claim 1 , and a substitution at position 201 from tyrosine to alanine (Y201A).4. The pyruvate dehydrogenase variant of claim 1 , wherein the amino acid substitution in the region of amino acids at positions from 415 to 440 of SEQ ID NO: 1 is selected from the group consisting of amino acids at positions 418 claim 1 , 428 claim 1 , 432 claim 1 , 435 claim 1 , and 438.5. The pyruvate dehydrogenase variant of claim 1 , wherein the amino acid substitution in the region of amino acids at positions from 415 to 440 of SEQ ID NO: 1 is selected from the group consisting of a substitution at position 418 from tyrosine to histidine (Y418H) claim 1 , a substitution at position 428 from asparagine to alanine (N428A) claim 1 , a substitution at position 432 from glutamine to glutamic ...

Gold Optimized CAR T-cells

Control Devices are disclosed including RNA destabilizing elements (RDE), RNA control devices, and destabilizing elements (DE) combined with Chimeric Antigen Receptors (CARs) or other transgenes in eukaryotic cells. Multicistronic vectors are also disclosed for use in engineering host eukaryotic cells with the CARs and transgenes under the control of the control devices. These control devices can be used to optimize expression of CARs in the eukaryotic cells so that, for example, effector function is optimized. CARs and transgene payloads can also be engineered into eukaryotic cells so that the transgene payload is expressed and delivered after stimulation of the CAR on the eukaryotic cell.