Patent classifications
C12Y101/01035
Hydroxyacyl-coenzyme A dehydrogenase gene, an acyl-coenzyme A thiolase gene, genetically engineered strains and a use thereof
The present invention provides a hydroxyacyl-coenzyme A dehydrogenase gene, an acyl-coenzyme A thiolase gene, genetically engineered strains and a use thereof. The hydroxyacyl-coenzyme A dehydrogenase gene encodes a protein (i) or (ii) as follows: (i) having an amino acid sequence according to SEQ ID NO 2; (ii) derived by substituting, deleting or inserting one or more amino acids in the amino acid sequence defined by (i) and having the same function as that of the protein of (i). The present invention constructs genetically engineered Mycobacterium strains lacking of a hydroxyacyl-coenzyme A dehydrogenase gene or an acyl-coenzyme A thiolase gene, which are used in the preparation of steroidal compounds, such as 1,4-BNA, 4-BNA, 9-OH-BNA, etc. Further, the invention improves the production efficiency and product quality of steroidal drug, improves the utilization of drug precursors, reduces the production costs, and provides the advantages of mild reaction conditions, environmentally friendly, and high economic and social benefits.
TRANSFORMANT THAT PRODUCES COPOLYMERIZED PHA CONTAINING 3HH UNIT, AND METHOD FOR PRODUCING SAID PHA
Provided are a transformant that produces a copolymerized PHA containing 3HH units in a higher composition proportion; and a method for producing a copolymerized PHA, using this transformant. The transformant is a transformant that produces a copolymerized PHA containing 3HH units, in which a gene encoding an enzyme having trans-2-enoyl-CoA hydratase activity and (R)-3-hydroxyacyl-CoA dehydrogenase activity is introduced into a prokaryotic microorganism having a PHA synthetase gene capable of synthesizing the copolymerized PHA containing the 3HH units. The method is a method for producing a copolymerized PHA containing 3HH units, which includes a step of culturing this transformant.
Primary alcohol producing organisms
The invention provides a non-naturally occurring microbial organism having a microbial organism having at least one exogenous gene insertion and/or one or more gene disruptions that confer production of primary alcohols. A method for producing long chain alcohols includes culturing these non-naturally occurring microbial organisms.
Production of 4,6-dihydroxy-2-oxo-hexanoic acid
Provided herein are methods, compositions, and non-naturally occurring microbial organism for preparing compounds such as1-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, ?-Caprolactone, 6-amino-hexanoic acid, ?-Caprolactam, hexamethylenediamine, linear fatty acids and linear fatty alcohols that are between 7-25 carbons long, linear alkanes and linear ?-alkenes that are between 6-24 carbons long, sebacic acid and dodecanedioic acid comprising: a) converting a C.sub.N aldehyde and pyruvate to a C.sub.N+3 ?-hydroxyketone intermediate through an aldol addition; and b) converting the C.sub.N+3 ?-hydroxyketone intermediate to the compounds through enzymatic steps, or a combination of enzymatic and chemical steps.
NOVEL METHOD FOR PREPARING POLY(3-HYDROXYBUTYRATE-CO-HYDROXYBUTYRATE)
The present disclosure relates to a novel method for preparing poly(3-hydroxybutyrate-co-4-hydroxybutyrate), a microorganism using the biosynthetic pathway of poly(3-hydroxybutyrate-co-4-hydroxybutyrate) of the present disclosure, a composition for producing poly(3-hydroxybutyrate-co-4-hydroxybutyrate), and a method for regulating the 4-hydroxybutyrate content of poly(3-hydroxybutyrate-co-4-hydroxybutyrate).
PRODUCTION OF POLYHYDROXYALKANOATES WITH A DEFINED COMPOSITION FROM AN UNRELATED CARBON SOURCE
Cells and methods for producing polyhydroxyalkanoates. The cells comprise one or more recombinant genes selected from an R-specific enoyl-CoA hydratase gene, a PHA polymerase gene, a thioesterase gene, and an acyl-CoA-synthetase gene. The cells further have one or more genes functionally deleted. The functionally deleted genes include such genes as an enoyl-CoA hydratase gene, a 3-hydroxyacyl-CoA dehydrogenase, and a 3-ketoacyl-CoA thiolase gene. The recombinant cells are capable of using producing polyhydroxyalkanoates with a high proportion of monomers having the same carbon length from non-lipid substrates, such as carbohydrates.
Microorganisms and methods for the production of fatty acids and fatty acid derived products
This invention relates to metabolically engineered microorganism strains, such as bacterial strains, in which there is an increased utilization of malonyl-CoA for production of a fatty acid or fatty acid derived product, wherein the modified microorganism produces fatty acyl-CoA intermediates via a malonyl-CoA dependent but malonyl-ACP independent mechanism.
ITERATIVE PLATFORM FOR THE SYNTHESIS OF ALPHA FUNCTIONALIZED PRODUCTS
The use of microorganisms to make alpha-functionalized chemicals and fuels, (e.g. alpha-functionalized carboxylic acids, alcohols, hydrocarbons, amines, and their beta-, and omega-functionalized derivatives), by utilizing an iterative carbon chain elongation pathway that uses functionalized extender units. The core enzymes in the pathway include thiolase, dehydrogenase, dehydratase and reductase. Native or engineered thiolases catalyze the condensation of either unsubstituted or functionalized acyl-CoA primers with an alpha-functionalized acetyl-CoA as the extender unit to generate alpha-functionalized -keto acyl-CoA. Dehydrogenase converts alpha-functionalized -keto acyl-CoA to alpha-functionalized -hydroxy acyl-CoA. Dehydratase converts alpha-functionalized -hydroxy acyl-CoA to alpha-functionalized enoyl-CoA. Reductase converts alpha-functionalized enoyl-CoA to alpha-functionalized acyl-CoA. The platform can be operated in an iterative manner (i.e. multiple turns) by using the resulting alpha-functionalized acyl-CoA as primer and the aforementioned alpha-functionalized extender unit in subsequent turns of the cycle. Termination pathways acting on any of the four alpha-functionalized CoA thioester intermediates terminate the platform and generate various alpha-functionalized carboxylic acids, alcohols and amines with different -reduction degree.
HYDROXYACYL-COENZYME A DEHYDROGENASE GENE, AN ACYL-COENZYME A THIOLASE GENE, GENETICALLY ENGINEERED STRAINS AND A USE THEREOF
The present invention provides a hydroxyacyl-coenzyme A dehydrogenase gene, an acyl-coenzyme A thiolase gene, genetically engineered strains and a use thereof. The hydroxyacyl-coenzyme A dehydrogenase gene encodes a protein (i) or (ii) as follows: (i) having an amino acid sequence according to SEQ ID NO 2; (ii) derived by substituting, deleting or inserting one or more amino acids in the amino acid sequence defined by (i) and having the same function as that of the protein of (i). The present invention constructs genetically engineered Mycobacterium strains lacking of a hydroxyacyl-coenzyme A dehydrogenase gene or an acyl-coenzyme A thiolase gene, which are used in the preparation of steroidal compounds, such as 1,4-BNA, 4-BNA, 9-OH-BNA, etc . . . Further, the invention improves the production efficiency and product quality of steroidal drug, improves the utilization of drug precursors, reduces the production costs, and provides the advantages of mild reaction conditions, environmentally friendly, and high economic and social benefits.
METHODS AND MATERIALS FOR BIOSYNTHESIZING MULTIFUNCTIONAL, MULTIVARIATE MOLECULES VIA CARBON CHAIN MODIFICATION
This document describes biochemical pathways for producing a difunctional product having an odd number of carbon atoms in vitro or in a recombinant host, or salts or derivatives thereof, by forming two terminal functional groups selected from carboxyl, amine, formyl, and hydroxyl groups in an aliphatic carbon chain backbone having an odd number of carbon atoms synthesized from (i) acetyl-CoA and propanedioyl-CoA via one or more cycles of methyl ester shielded carbon chain elongation or (ii) propanedioyl-[acp] via one or more cycles of methyl ester shielded carbon chain elongation. The biochemical pathways and metabolic engineering and cultivation strategies described herein rely on enzymes or homologs accepting methyl ester shielded aliphatic carbon chain backbones and maintaining the methyl ester shield for at least one further enzymatic step following one or more cycles of methyl ester shielded carbon chain elongation.