Pyruvate oxidase
| pyruvate oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.2.3.3 | ||||||||
| CAS number | 9001-96-1 | ||||||||
| 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 oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction
- pyruvate + phosphate + O2 acetyl phosphate + CO2 + H2O2
The 3 substrates of this enzyme are pyruvate, phosphate, and O2, whereas its 3 products are acetyl phosphate, CO2, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (phosphorylating). Other names in common use include pyruvic oxidase, and phosphate-dependent pyruvate oxidase. This enzyme participates in pyruvate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.
Structural studies
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1POW, 1POX, 1V5E, 1V5F, 1V5G, 1Y9D, 2DJI, 2EZ4, 2EZ8, 2EZ9, 2EZT, and 2EZU.
References
- Williams FR, Hager LP (1966). "Crystalline flavin pyruvate oxidase from Escherichia coli. I Isolation and properties of the flavoprotein". Arch. Biochem. Biophys. 116 (1): 168–76. doi:10.1016/0003-9861(66)90025-7. PMID 5336022.
- Tittmann K, Wille G, Golbik R, Weidner A, Ghisla S, Hubner G (2005). "Radical phosphate transfer mechanism for the thiamin diphosphate- and FAD-dependent pyruvate oxidase from Lactobacillus plantarum Kinetic coupling of intercofactor electron transfer with phosphate transfer to acetyl-thiamin diphosphate via a transient FAD semiquinone/hydroxyethyl-ThDP radical pair". Biochemistry. 44 (40): 13291–303. doi:10.1021/bi051058z. PMID 16201755.