EC |
1.2.3.3 |
Accepted name: |
pyruvate oxidase |
Reaction: |
pyruvate + phosphate + O2 = acetyl phosphate + CO2 + H2O2 |
Glossary: |
thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium |
Other name(s): |
pyruvic oxidase; phosphate-dependent pyruvate oxidase |
Systematic name: |
pyruvate:oxygen 2-oxidoreductase (phosphorylating) |
Comments: |
A flavoprotein (FAD) requiring thiamine diphosphate. Two reducing equivalents are transferred from the resonant carbanion/enamine forms of 2-hydroxyethyl-thiamine-diphosphate to the adjacent flavin cofactor, yielding 2-acetyl-thiamine diphosphate (AcThDP) and reduced flavin. FADH2 is reoxidized by O2 to yield H2O2 and FAD and AcThDP is cleaved phosphorolytically to acetyl phosphate and thiamine diphosphate [2]. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9001-96-1 |
References: |
1. |
Williams, F.R. and Hager, L.P. Crystalline flavin pyruvate oxidase from Escherichia coli. I. Isolation and properties of the flavoprotein. Arch. Biochem. Biophys. 116 (1966) 168–176. [PMID: 5336022] |
2. |
Tittmann, K., Wille, G., Golbik, R., Weidner, A., Ghisla, S. and Hübner, G. 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 (2005) 13291–13303. [DOI] [PMID: 16201755] |
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[EC 1.2.3.3 created 1961] |
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