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Oxalate oxidase

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oxalate oxidase
Oxalate oxidase 1 dimer, Barley
Identifiers
EC no.1.2.3.4
CAS no.9031-79-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, oxalate oxidase (EC 1.2.3.4) is an oxalate degrading enzyme that catalyzes the chemical reaction:

 
O2
H2O2
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
O2
H2O2
 
2 CO2
 

The two substrates of this enzyme are oxalic acid and oxygen. Its products are carbon dioxide and hydrogen peroxide.[1][2][3]

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.[4]

Structural studies

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As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1FI2, 2ET1, 2ET7, and 2ETE.

References

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  1. ^ Enzyme 1.2.3.4 at KEGG Pathway Database.
  2. ^ 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.
  3. ^ 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.
  4. ^ 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.