Thiosulfate dehydrogenase (quinone)
| thiosulfate dehydrogenase (quinone) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.8.5.2 | ||||||||
| 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 thiosulfate dehydrogenase (quinone) (EC 1.8.5.2) is an enzyme that catalyzes the chemical reaction
- 2 thiosulfate + 2 6-decylubiquinone tetrathionate + 2 6-decylubiquinol
Thus, the two substrates of this enzyme are thiosulfate and 6-decylubiquinone, whereas its two products are tetrathionate and 6-decylubiquinol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a quinone or similar compound as acceptor. The systematic name of this enzyme class is thiosulfate:6-decylubiquinone oxidoreductase. Other names in common use include thiosulfate:quinone oxidoreductase, thiosulphate:quinone oxidoreductase, thiosulfate oxidoreductase, tetrathionate-forming, and TQO.
References
- Muller FH, Bandeiras TM, Urich T, Teixeira M, Gomes CM, Kletzin A (2004). "Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate:quinone oxidoreductase". Mol. Microbiol. 53 (4): 1147–60. doi:10.1111/j.1365-2958.2004.04193.x. PMID 15306018.
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