C12P13/12

CYSTEINE POLYSULFIDATION AND MITOCHONDRIAL BIOENERGETICS REGULATED BY CYSTEINYL-tRNA SYNTHETASE
20210403963 · 2021-12-30 ·

A method of synthesize cysteine hydropersulfide (CysSSH) includes taking a substrate L-cysteine, and performing a reaction catalyzed by cysteinyl-tRNA synthetases (CARSs).

CYSTEINE POLYSULFIDATION AND MITOCHONDRIAL BIOENERGETICS REGULATED BY CYSTEINYL-tRNA SYNTHETASE
20210403963 · 2021-12-30 ·

A method of synthesize cysteine hydropersulfide (CysSSH) includes taking a substrate L-cysteine, and performing a reaction catalyzed by cysteinyl-tRNA synthetases (CARSs).

ENGINEERED BIOSYNTHETIC PATHWAYS FOR PRODUCTION OF L-HOMOCYSTEINE BY FERMENTATION

The present disclosure describes the engineering of microbial cells for fermentative production of L-homocysteine and provides novel engineered microbial cells and cultures, as well as related L-homocysteine production methods.

ENGINEERED BIOSYNTHETIC PATHWAYS FOR PRODUCTION OF L-HOMOCYSTEINE BY FERMENTATION

The present disclosure describes the engineering of microbial cells for fermentative production of L-homocysteine and provides novel engineered microbial cells and cultures, as well as related L-homocysteine production methods.

IMPROVED CYSTEINE-PRODUCING STRAINS
20230265473 · 2023-08-24 · ·

Genetically modified microorganism strains for the fermentative production of cysteine provide higher yields of L-cysteine or L-cystine during fermentation. Cysteine production is improved in the genetically modified microorganism strains by attenuating or inactivating phosphoenolpyruvate synthase enzyme activity, alone or in combination with the overexpression of efflux proteins and proteins that reduce feedback inhibition by cysteine and by serine.

IMPROVED CYSTEINE-PRODUCING STRAINS
20230265473 · 2023-08-24 · ·

Genetically modified microorganism strains for the fermentative production of cysteine provide higher yields of L-cysteine or L-cystine during fermentation. Cysteine production is improved in the genetically modified microorganism strains by attenuating or inactivating phosphoenolpyruvate synthase enzyme activity, alone or in combination with the overexpression of efflux proteins and proteins that reduce feedback inhibition by cysteine and by serine.

Enhanced metabolite-producing yeast

Metabolites produced by a microorganism using more particularly oxaloacetate as substrate or co-substrate upstream in the biosynthesis pathway. There is indeed a need in the art for transformed, in particular recombinant, microorganisms having at least an increased ability to produce oxaloacetate, thus allowing an increased capacity to produce oxaloacetate-derived amino acids and amino acid derivatives, the oxaloacetate-derived amino acids and amino acid derivatives being termed oxaloacetate derivatives. The solution is the use of a genetically modified yeast including many modifications as described in the present text.

MODIFIED POLYPEPTIDE WITH ATTENUATED ACTIVITY OF CITRATE SYNTHASE AND METHOD FOR PRODUCING L-AMINO ACID USING THE SAME
20210355514 · 2021-11-18 ·

The present disclosure relates to a modified polypeptide with attenuated activity of citrate synthase and a method for producing an aspartate-derived L-amino acid using the modified polypeptide.

MODIFIED POLYPEPTIDE WITH ATTENUATED ACTIVITY OF CITRATE SYNTHASE AND METHOD FOR PRODUCING L-AMINO ACID USING THE SAME
20210355514 · 2021-11-18 ·

The present disclosure relates to a modified polypeptide with attenuated activity of citrate synthase and a method for producing an aspartate-derived L-amino acid using the modified polypeptide.

Method of Producing L-Amino Acids

A method is described for producing an L-amino acid including the steps of cultivating in a culture medium an L-amino acid-producing bacterium belonging to the family Enterobacteriaceae to produce and accumulate the L-amino acid in the culture medium, cells of the bacterium, or both, and collecting the L-amino acid from the culture medium, the cells, or both, wherein said bacterium has been modified to overexpress a gene encoding a periplasmic adaptor protein.