Pyranose oxidase
In enzymology, a pyranose oxidase (EC 1.1.3.10) is an enzyme that catalyzes the chemical reaction
- D-glucose + O2 2-dehydro-D-glucose + H2O2
| pyranose oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Pyranose oxidase tetramer, Trametes ochracea | |||||||||
| Identifiers | |||||||||
| EC number | 1.1.3.10 | ||||||||
| CAS number | 37250-80-9 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are D-glucose and O2, whereas its two products are 2-dehydro-D-glucose 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 pyranose:oxygen 2-oxidoreductase. Other names in common use include glucose 2-oxidase, and pyranose-2-oxidase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, FAD.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1TT0, 1TZL, 2F5V, 2F6C, 2IGK, 2IGM, 2IGN, and 2IGO.
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References
- Janssen FW, Ruelius HW (1968). "Carbohydrate oxidase, a novel enzyme from Polyporus obtusus. II Specificity and characterization of reaction products". Biochim. Biophys. Acta. 167 (3): 501–10. doi:10.1016/0005-2744(68)90040-5. PMID 5722278.
- Machida Y, Nakanishi T (1984). "Purification and properties of pyranose oxidase from Coriolus versicolor". Agric. Biol. Chem. 48 (10): 2463–2470. doi:10.1271/bbb1961.48.2463.
- Neidleman SL, Amon WF Jr, Geigert J (1981). "Process for the production of fructose". Chem. Abstr. 94: 20737.
- Ruelius HW, Kerwin RM, Janssen FW (1968). "Carbohydrate oxidase, a novel enzyme from Polyporus obtusus. I Isolation and purification". Biochim. Biophys. Acta. 167 (3): 493–500. doi:10.1016/0005-2744(68)90039-9. PMID 5725162.
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