Pyruvate oxidase

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

pyruvate + phosphate + O₂ ${\displaystyle \rightleftharpoons }$ acetyl phosphate + CO₂ + H₂O₂

pyruvate oxidase
Identifiers
EC no.	1.2.3.3
CAS no.	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 / QuickGO
Search PMC articles PubMed articles NCBI proteins

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.