Pyruvate dehydrogenase (acetyl-transferring)

In enzymology, a pyruvate dehydrogenase (acetyl-transferring) is an enzyme that catalyzes the chemical reaction


 * pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine $$\rightleftharpoons$$ [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2

Thus, the two substrates of this enzyme are pyruvate and [dihydrolipoyllysine-residue 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:[dihydrolipoyllysine-residue 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.