Galactose oxidase
| galactose oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.3.9 | ||||||||
| CAS number | 9028-79-9 | ||||||||
| 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 galactose oxidase (EC 1.1.3.9) is an enzyme that catalyzes the chemical reaction
- D-galactose + O2
D-galacto-hexodialdose + H2O2
Thus, the two substrates of this enzyme are D-galactose and O2, whereas its two products are D-galacto-hexodialdose and H2O2.
Function
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. It employs two cofactors, copper and an active site amino acid derived post-translational modification involving the covalent cross-linking of Cys228 and Tyr272 and which represents the site of the catalytic free radical.
Nomenclature
The systematic name of this enzyme class is D-galactose:oxygen 6-oxidoreductase. Other names in common use include D-galactose oxidase, and beta-galactose oxidase.
References
- Avigad G, Amaral D, Asensio C, Horecker BL (1962). "The D-galactose oxidase of Polyporus circinatus". J. Biol. Chem. 237: 2736–43. PMID 13863403.