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 | ||||||
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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.
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 D-galactose:oxygen 6-oxidoreductase. Other names in common use include D-galactose oxidase, and beta-galactose oxidase. 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.
[edit] Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1GOF, 1GOG, 1GOH, 1K3I, 1T2X, 2EIB, 2EIC, 2EID, and 2EIE.
[edit] 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.
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D-galacto-hexodialdose + H2O2