Pyruvate dehydrogenase (acetyl-transferring)

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pyruvate dehydrogenase (acetyl-transferring)
1ni4.jpg
Pyruvate dehydrogenase E1 heterotetramer, Human
Identifiers
EC number 1.2.4.1
CAS number 9014-20-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, a pyruvate dehydrogenase (acetyl-transferring) (EC 1.2.4.1) 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.

References[edit]

  • OCHOA S (1954). "Enzymic mechanisms in the citric acid cycle". Adv. Enzymol. Relat. Subj. Biochem. 15: 183–270. PMID 13158180. 
  • Scriba P; Holzer H (1961). "Gewinnung von alphaHydroxyathyl-2-thiaminpyrophosphat mit Pyruvatoxydase aus Schweineherzmuskel". Biochem. Z. 334: 473–486. 
  • Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions". Annu. Rev. Biochem. 69 (1): 961–1004. PMID 10966480. doi:10.1146/annurev.biochem.69.1.961.