EC 1.2.3.3 - Pyruvate oxidase

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IntEnz Enzyme Nomenclature
EC 1.2.3.3

Names

Accepted name:
pyruvate oxidase
Other names:
pyruvic oxidase
phosphate-dependent pyruvate oxidase
Systematic name:
pyruvate:oxygen 2-oxidoreductase (phosphorylating)

Reaction

Cofactors

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00166
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047112
CAS Registry Number: 9001-96-1
UniProtKB/Swiss-Prot:

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: 168-176 (1966). [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: 13291-13303 (2005). [PMID: 16201755]

[EC 1.2.3.3 created 1961, modified 2006]