Pyruvate dehydrogenase (cytochrome)
In enzymology, a pyruvate dehydrogenase (cytochrome) (EC 1.2.2.2) is an enzyme that catalyzes the chemical reaction
- pyruvate + ferricytochrome b1 + H2O acetate + CO2 + ferrocytochrome b1
pyruvate dehydrogenase (cytochrome) | |||||||||
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Identifiers | |||||||||
EC no. | 1.2.2.2 | ||||||||
CAS no. | 9079-84-9 | ||||||||
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 / QuickGO | ||||||||
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The 3 substrates of this enzyme are pyruvate, ferricytochrome b1, and H2O, whereas its 3 products are acetate, CO2, and ferrocytochrome b1.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is pyruvate:ferricytochrome-b1 oxidoreductase. Other names in common use include pyruvate dehydrogenase, pyruvic dehydrogenase, pyruvic (cytochrome b1) dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, and pyruvate oxidase (ambiguous). This enzyme participates in pyruvate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.
References
- Williams FR; Hager LP (1961). "A crystalline flavin pyruvate oxidase". J. Biol. Chem. 236: PC36–PC37.
- Koland JG, Gennis RB (1982). "Identification of an active site cysteine residue in Escherichia coli pyruvate oxidase". J. Biol. Chem. 257 (11): 6023–7. PMID 7042705.