Home  |  Contact
Due to work on this service, it may not be fully operational on Wednesday March 20 between 1.30 pm and 2.30 pm CEST. Apologies for the inconvenience.

A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC 1.2.3.3

Accepted Name
Pyruvate oxidase.
Alternative Name(s)
Phosphate-dependent pyruvate oxidase.
Pyruvic oxidase.
Reaction catalysed
Pyruvate + phosphate + O(2) <=> acetyl phosphate + CO(2) + H(2)O(2)
Cofactor(s)
FAD; Thiamine diphosphate.
Comment(s)
  • 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.
  • FADH is reoxidized by O(2) to yield H(2)O(2) and FAD and AcThDP is cleaved phosphorolytically to acetyl phosphate and thiamine diphosphate.
Cross-references
PROSITEPDOC00166
BRENDA1.2.3.3
EC2PDB1.2.3.3
ExplorEnz1.2.3.3
PRIAM enzyme-specific profiles1.2.3.3
KEGG Ligand Database for Enzyme Nomenclature1.2.3.3
IUBMB Enzyme Nomenclature1.2.3.3
IntEnz1.2.3.3
MEDLINEFind literature relating to 1.2.3.3
MetaCyc1.2.3.3
UniProtKB/Swiss-Prot
P37063, POXB_LACPL;  Q54970, POXB_STRPN;  

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.2.3.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.2.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-