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2 results about "Pyruvate formate lyase" patented technology

In enzymology, formate C-acetyltransferase (pyruvate formate lyase) (EC 2.3.1.54) is an enzyme. Pyruvate formate lyase is found in Escherichia coli and other organisms. It helps regulate anaerobic glucose metabolism. Using radical non-redox chemistry, it catalyzes the reversible conversion of pyruvate and coenzyme-A into formate and acetyl-CoA.

Recombinant microorganism capable of growing using only carbon dioxide and formic acid, and method for producing useful substances using the recombinant microorganism

ActiveDE102021207101B4BacteriaHydrolasesAcyl CoA dehydrogenasePhosphoenolpyruvic acid
Recombinant microorganism in which a gene encoding a transcriptional repressor of the glycine cleavage system, pyruvate formate lyase or phosphoglycerate dehydrogenase, is attenuated or deleted from a host microorganism with a formic acid assimilation pathway, a ppsR gene encoding a phosphoenolpyruvate synthase regulatory protein, or a purT gene encoding a phosphoribosylglycinamide formyltransferase, is attenuated or deleted, a gcvTHP gene, consisting of the gcvT gene, the gcvH gene and the gcvP gene, which encodes an enzyme involved in a glycine cleavage system reaction in which host microorganism with the formic acid assimilation pathway is highly expressed, and a gene encoding formate tetrahydrofolate ligase, methenyl tetrahydrofolate cyclohydrolase or methylene tetrahydrofolate dehydrogenase is introduced into the host microorganism via the formic acid assimilation pathway.
Owner:KOREA ADVANCED INST OF SCI & TECH

Use of modified Escherichia coli and its L-amino acids in fermentation production

PendingJP2026521933AEscherichia coliTransgene
This paper discloses the use of modified Escherichia coli and its L-amino acid fermentation production. Specifically, it discloses the use of pyruvate formate lyase, alcohol dehydrogenase, branched-chain amino acid transaminase derived from Escherichia coli, branched-chain amino acid transaminase derived from Bacillus subtilis, thiamine phosphate synthase, and maleate dehydrogenase in the construction of genetically modified bacteria that produce L-amino acids. Experiments have shown that by knocking out the genes encoding pyruvate formate lyase, alcohol dehydrogenase, branched-chain amino acid transaminase derived from Escherichia coli, thiamine phosphate synthase, and maleate dehydrogenase in E. coli capable of producing L-amino acids, and introducing the gene encoding branched-chain amino acid transaminase derived from Bacillus subtilis, recombinant bacteria favorable for L-amino acid accumulation can be obtained. These recombinant bacteria can significantly increase L-amino acid production and reduce costs, which is of great significance in accelerating the industrialization process of L-amino acids.
Owner:NINGXIA EPPEN BIOTECH CO LTD