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Pyruvate dehydrogenase (acetyl-transferring) : ウィキペディア英語版 | Pyruvate dehydrogenase (acetyl-transferring)
In enzymology, a pyruvate dehydrogenase (acetyl-transferring) () is an enzyme that catalyzes the chemical reaction :pyruvate + (acetyltransferase ) lipoyllysine (acetyltransferase ) S-acetyldihydrolipoyllysine + CO2 Thus, the two substrates of this enzyme are pyruvate and (acetyltransferase ) lipoyllysine, whereas its 3 products are dihydrolipoyllysine-residue acetyltransferase, S-acetyldihydrolipoyllysine, and CO2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a disulfide as acceptor. The systematic name of this enzyme class is pyruvate:(acetyltransferase )-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-acetylating). Other names in common use include MtPDC (mitochondrial pyruvate dehydogenase complex), pyruvate decarboxylase, pyruvate dehydrogenase, pyruvate dehydrogenase (lipoamide), pyruvate dehydrogenase complex, pyruvate:lipoamide 2-oxidoreductase (decarboxylating and, acceptor-acetylating), pyruvic acid dehydrogenase, and pyruvic dehydrogenase. This enzyme participates in 5 metabolic pathways: glycolysis / gluconeogenesis, alanine and aspartate metabolism, valine, leucine and isoleucine biosynthesis, pyruvate metabolism, and butanoate metabolism. It employs one cofactor, thiamin diphosphate. ==Structural studies==
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , and .
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