Pyruvate oxidase

From Wikipedia, the free encyclopedia

In enzymology, a pyruvate oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction

pyruvate + phosphate + O₂ $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 1.2.3.3
BRENDA references for 1.2.3.3 (Recommended.)
PubMed references for 1.2.3.3
PubMed Central references for 1.2.3.3
Google Scholar references for 1.2.3.3
Williams FR, Hager LP (1966). "Crystalline flavin pyruvate oxidase from Escherichia coli. I Isolation and properties of the flavoprotein". Arch. Biochem. Biophys. 116: 168–76. 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: 13291–303. PMID 16201755.