Sulfur dioxygenase
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+
Sulfur dioxygenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.13.11.18 | ||||||||
CAS no. | 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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This enzyme contains iron.
In humans, sulfur dioxygenase is needed to detoxify sulfide.[3]
References
- Suzuki I, Silver M (July 1966). "The initial product and properties of the sulfur-oxidizing enzyme of thiobacilli". Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation. 122 (1): 22–33. doi:10.1016/0926-6593(66)90088-9. PMID 5968172.
- Rohwerder T, Sand W (July 2003). "The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp". Microbiology. 149 (Pt 7): 1699–710. doi:10.1099/mic.0.26212-0. PMID 12855721.
- Viscomi C, Burlina AB, Dweikat I, Savoiardo M, Lamperti C, Hildebrandt T, Tiranti V, Zeviani M (August 2010). "Combined treatment with oral metronidazole and N-acetylcysteine is effective in ethylmalonic encephalopathy". Nature Medicine. 16 (8): 869–71. doi:10.1038/nm.2188. hdl:11577/3321433. PMID 20657580.
External links
- Sulfur+dioxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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