Pyruvate dehydrogenase (acetyl-transferring)

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pyruvate dehydrogenase (acetyl-transferring)
Pyruvate dehydrogenase E1 heterotetramer, Human
EC number
CAS number 9014-20-4
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

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

pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine [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[edit]

As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1L8A, 1NI4, 1RP7, 1W85, 1W88, 2G25, 2G28, 2G67, 2IEA, 2OZL, 2QTA, and 2QTC.


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