Sulfur dioxygenase
Sulfur dioxygenase | |||||||||
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Identifiers | |||||||||
EC number | 1.13.11.18 | ||||||||
CAS number | 37256-58-9 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Sulfur dioxygenase (EC 1.13.11.18, sulfur oxygenase, sulfur:oxygen oxidoreductase) is an enzyme with systematic name S-sulfanylglutathione:oxygen oxidoreductase.[1][2] This enzyme catalyses the following chemical reaction
- sulfur + O2 + H2O sulfite + 2 H+ (overall reaction)
- (1a) glutathione + sulfur S-sulfanylglutathione (spontaneous reaction)
- (1b) S-sulfanylglutathione + O2 + H2O glutathione + sulfite + 2 H+
This enzyme contains iron.
In humans, sulfur dioxygenase is needed to detoxify sulfide.[3]
References
- ↑ Suzuki, I.; Silver, M. (1966). "The initial product and properties of the sulfur-oxidizing enzyme of thiobacilli". Biochim. Biophys. Acta. 122: 22–33. PMID 5968172. doi:10.1016/0926-6593(66)90088-9.
- ↑ Rohwerder, T.; Sand, W. (2003). "The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp". Microbiology. 149: 1699–1710. PMID 12855721. doi:10.1099/mic.0.26212-0.
- ↑ Viscomi, C.; Burlina, A.B.; Dweikat, I.; Savoiardo, M.; Lamperti, C.; Hildebrandt, T.; Tiranti, V.; Zeviani, M. (2010). "Combined treatment with oral metronidazole and N-acetylcysteine is effective in ethylmalonic encephalopathy". Nat Med. 16: 869–71. PMID 20657580. doi:10.1038/nm.2188.
External links
- Sulfur dioxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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