Dimethyl sulfide:cytochrome c2 reductase
| Dimethyl sulfide:cytochrome c2 reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.8.2.4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Dimethyl sulfide:cytochrome c2 reductase (EC 1.8.2.4, Ddh (gene)) is an enzyme with systematic name dimethyl sulfide:cytochrome-c2 oxidoreductase.[1][2] This enzyme catalyses the following chemical reaction
- dimethyl sulfide + 2 ferricytochrome c2 + H2O dimethyl sulfoxide + 2 ferrocytochrome c2 + 2 H+
The enzyme from the bacterium Rhodovulum sulfidophilum binds molybdopterin guanine dinucleotide, heme b and [4Fe-4S] clusters.
References
- ↑ Hanlon, S.P.; Toh, T.H.; Solomon, P.S.; Holt, R.A.; McEwan, A.G. (1996). "Dimethylsulfide:acceptor oxidoreductase from Rhodobacter sulfidophilus. The purified enzyme contains b-type haem and a pterin molybdenum cofactor". Eur. J. Biochem. 239: 391–396. doi:10.1111/j.1432-1033.1996.0391u.x. PMID 8706745.
- ↑ McDevitt, C.A.; Hugenholtz, P.; Hanson, G.R.; McEwan, A.G. (2002). "Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes". Mol. Microbiol. 44: 1575–1587. doi:10.1046/j.1365-2958.2002.02978.x. PMID 12067345.
External links
- Dimethyl sulfide:cytochrome c2 reductase at the US National Library of Medicine Medical Subject Headings (MeSH)
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