Malate oxidase
| malate oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.3.3 | ||||||||
| CAS number | 9028-73-3 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a malate oxidase (EC 1.1.3.3) is an enzyme that catalyzes the chemical reaction
- (S)-malate + O2 oxaloacetate + H2O2
Thus, the two substrates of this enzyme are (S)-malate and O2, whereas its two products are oxaloacetate and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is (S)-malate:oxygen oxidoreductase. Other names in common use include FAD-dependent malate oxidase, malic oxidase, and malic dehydrogenase II. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD.
References
- COHN DV (1958). "The enzymatic formation of oxalacetic acid by nonpyridine nucleotide malic dehydrogenase of Micrococcus lysodeikticus". J. Biol. Chem. 233 (2): 299–304. PMID 13563491.
- Narindrasorasak S, Goldie AH, Sanwal BD (1979). "Characteristics and regulation of a phospholipid-activated malate oxidase from Escherichia coli". J. Biol. Chem. 254 (5): 1540–5. PMID 368072.
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