| thiol oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.8.3.2 | ||||||||
| CAS no. | 9029-39-4 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a thiol oxidase (EC 1.8.3.2) is an enzyme that catalyzes the chemical reaction
- 4 R'C(R)SH + O2 2 R'C(R)S-S(R)CR' + 2 H2O
2 R'C(R)S-S(R)CR' + 2 H2OThus, the two substrates of this enzyme are R'C(R)SH and O2, whereas its two products are R'C(R)S-S(R)CR' and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with oxygen as acceptor. The systematic name of this enzyme class is thiol:oxygen oxidoreductase. This enzyme is also called sulfhydryl oxidase.
References
- AURBACH GD, JAKOBY WB (1962). "The multiple functions of thiooxidase". J. Biol. Chem. 237: 565–8. PMID 13863296.
- NEUFELD HA, GREEN LF, LATTERELL FM, WEINTRAUB RL (1958). "Thioxidase, a new sulfhydryl-oxidizing enzyme from Piricularia oryzae and Polyporus versicolor". J. Biol. Chem. 232 (2): 1093–9. PMID 13549489.
| Oxidoreductases: sulfur oxidoreductases (EC 1.8) | |
|---|---|
| 1.8.1: NAD or NADP | |
| 1.8.2: cytochrome | |
| 1.8.3: oxygen | |
| 1.8.4: disulfide | |
| 1.8.5: quinone | |
| 1.8.98: Other, known | |
| 1.8.99: Other | |
| Enzymes | |
|---|---|
| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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