Oxalate oxidase
In enzymology, an oxalate oxidase (EC 1.2.3.4) is an oxalate degrading enzyme that catalyzes the chemical reaction:
- oxalate + O2 + 2 H+ 2 CO2 + H2O2
| oxalate oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Oxalate oxidase 1 dimer, Barley | |||||||||
| Identifiers | |||||||||
| EC no. | 1.2.3.4 | ||||||||
| CAS no. | 9031-79-2 | ||||||||
| 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 | ||||||||
| |||||||||
The 3 substrates of this enzyme are oxalate, O2, and H+, whereas its two products are 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 oxalate:oxygen oxidoreductase. Other names in common use include aero-oxalo dehydrogenase, and oxalic acid oxidase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It uses Manganese as a cofactor.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1FI2, 2ET1, 2ET7, and 2ETE.
References
- DATTA PK, MEEUSE BJ (1955). "Moss oxalic acid oxidase-a flavoprotein". Biochim. Biophys. Acta. 17 (4): 602–3. doi:10.1016/0006-3002(55)90436-4. PMID 13250021.
- Kotsira VP, Clonis YD (1997). "Oxalate oxidase from barley roots: purification to homogeneity and study of some molecular, catalytic, and binding properties". Arch. Biochem. Biophys. 340 (2): 239–49. doi:10.1006/abbi.1997.9896. PMID 9143327.
- Requena L, Bornemann S (1999). "Barley (Hordeum vulgare) oxalate oxidase is a manganese-containing enzyme". Biochem. J. 343 (Pt 1): 185–90. doi:10.1042/bj3430185. PMC 1220540. PMID 10493928.
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