C12Y101/01037

Method for the preparation of 2,4-dihydroxybutyrate

A method for the preparation of 2,4-dihydroxybutyric acid from homoserine includes a first step of conversion of the primary amino group of homoserine to a carbonyl group to obtain 2-oxo-4-hydroxybutyrate, and a second step of reduction of the obtained 2-oxo-4-hydroxybutyrate (OHB) to 2,4-dihydroxybutyrate.

Enhanced metabolite-producing yeast

Metabolites produced by a microorganism using oxaloacetate, pyruvate and/or acetyl-CoA as substrate or co-substrate upstream in the biosynthesis pathway, and more particularly using oxaloacetate. There is indeed a need in the art for transformed, in particular recombinant, microorganisms having at least an increased ability to produce oxaloacetate, pyruvate and/or acetyl-CoA, and in particular oxaloacetate, thus allowing an increased capacity to produce metabolites produced using oxaloacetate, pyruvate and/or acetyl-CoA as substrate or co-substrate upstream in the biosynthesis pathway, and in particular amino acids and their derivatives thereof, fatty acids, derivatives from the mevalonate pathway (in particular farnesyl, squalene, lanosterol, cholesterol and derivatives, and dolichols), flavonoides and/or polyketides. The solution proposed is the use of a genetically modified yeast comprising many modifications as described in the present text.

MICROORGANISMS AND METHODS FOR PRODUCTION OF SPECIFIC LENGTH FATTY ALCOHOLS AND RELATED COMPOUNDS
20220333143 · 2022-10-20 ·

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.

Mutant microorganism introduced with highly active malate dehydrogenase for producing succinic acid and method of producing succinic acid using the same

Disclosed are a mutant microorganism for producing succinic acid exhibiting improved activity of conversion of oxaloacetate to malate through the introduction of genes encoding a malate dehydrogenase, wherein an amino acid residue that interacts with a pyrophosphate moiety of NADH through an amide functional group of a main chain of malate dehydrogenase is glutamine (Gln), and a method of producing succinic acid using the same. The mutant microorganism producing succinic acid according to the present invention is capable of producing a high concentration of succinic acid at the highest productivity compared to other mutant microorganisms reported to date when the microorganism is cultured in a limited medium. In addition, the mutant microorganism is capable of producing succinic acid at higher productivity and product concentration through further advanced fermentation technology.

COMPOSITIONS AND METHODS FOR SUCCINATE PRODUCTION

The present application provides genetically modified yeast cell comprising an active succinate fermentation pathway, as well as methods of using these cells to produce succinate.

MULTI-ENZYME CONJUGATE, METHOD FOR PREPARING THE SAME AND METHOD FOR PREPARING ORGANIC COMPOUND USING THE SAME
20170356014 · 2017-12-14 ·

The present disclosure relates to a multi-enzyme conjugate, a method for preparing the same and a method for preparing an organic compound using the same. More particularly, a multi-enzyme conjugate exhibiting improved catalytic efficiency over respective free enzymes using site-specific incorporation of a clickable non-natural amino acid into the enzymes and two compatible click reactions, a method for preparing the same and a method for preparing an organic compound using the same may be provided.

METABOLIC ENGINEERING FOR ENHANCED SUCCINIC ACID BIOSYNTHESIS

Presented herein are biocatalysts and methods for the production of succinic acid from carbon sources. The biocatalysts include microbial cells that have been engineered to overexpress exogenously added genes that encode enzymes active in the reductive branch of the tricarboxylic acid (TCA) cycle.

Pharmaceutical composition for treating excessive lactate production and acidemia
11253495 · 2022-02-22 ·

Pharmaceuticals for treating patient with excessive lactate production and related acidemia are disclosed. Pharmaceuticals include glutamate, aspartate, BCAA, pyruvate, malate, oxaloacetate, α-ketoglutarate, AST, ALT, PLP, MDH and GPDH, Lodoxamite and Oxamate. The mechanism is that invented pharmaceuticals inhibit LDH and enhance malate/aspartate shuttle activity.

TRANSFORMANT, METHOD FOR MANUFACTURING SAME, AND METHOD FOR MANUFACTURING DICARBOXYLIC ACID HAVING 4 CARBON ATOMS

Provided is a transformant which uses Schizosaccharomyces pombe as a host, into which one or more foreign genes selected from the group consisting of a phosphoenolpyruvate carboxykinase gene and a pyruvate carboxylase gene are incorporated, and in which pdc2 genes of the Schizosaccharomyces pombe host have undergone deletion or deactivation, and a method for manufacturing a dicarboxylic acid having 4 carbon atoms by using the transformant.

Lactic Acid-Producing Hydrogenophilus Bacterium Transformant

A transformant obtained by introducing (a) a lactate dehydrogenase gene and/or (b) a malate/lactate dehydrogenase gene into a Hydrogenophilus bacterium efficiently produces lactic acid through use of carbon dioxide as a sole carbon source. Parageobacillus thermoglucosidasius ldh gene, Geobacillus kaustophilus ldh gene and Thermus thermophilus ldh gene of lactate dehydrogenases, and Thermus thermophilus mldh gene and Meiothermus ruber mldh-1 and mldh-2 genes of malate/lactate dehydrogenases are preferable in that they have good lactic acid production efficiency.