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Literature summary for 1.8.2.4 extracted from
- A mechanistic and electrochemical study of the interaction between dimethyl sulfide dehydrogenase and its electron transfer partner cytochrome c2 (2008), J. Biol. Inorg. Chem., 13, 1231-1238.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.021 | - |
ferricytochrome c2 | in 220 mM Tris-HCl pH 8.0, 22°C | Rhodovulum sulfidophilum |  |
| 0.053 | - |
Dimethyl sulfide | in 220 mM Tris-HCl pH 8.0, 22°C | Rhodovulum sulfidophilum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dimethyl sulfide + ferricytochrome c2 + H2O | Rhodovulum sulfidophilum | - |
dimethyl sulfoxide + ferrocytochrome c2 | - |
? | |
| dimethyl sulfide + ferricytochrome c2 + H2O | Rhodovulum sulfidophilum SH1 | - |
dimethyl sulfoxide + ferrocytochrome c2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodovulum sulfidophilum | - |
- |
- |
| Rhodovulum sulfidophilum SH1 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| ammonium sulfate precipitation, SP-Sepharose column chromatography, gel filtration | Rhodovulum sulfidophilum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dimethyl sulfide + ferricytochrome c2 + H2O | - |
Rhodovulum sulfidophilum | dimethyl sulfoxide + ferrocytochrome c2 | - |
? | |
| dimethyl sulfide + ferricytochrome c2 + H2O | DMS:ferrocytochrome oxidoreductase operates via a two-site ping-pong mechanism | Rhodovulum sulfidophilum | dimethyl sulfoxide + ferrocytochrome c2 | - |
? | |
| dimethyl sulfide + ferricytochrome c2 + H2O | - |
Rhodovulum sulfidophilum SH1 | dimethyl sulfoxide + ferrocytochrome c2 | - |
? | |
| dimethyl sulfide + ferricytochrome c2 + H2O | DMS:ferrocytochrome oxidoreductase operates via a two-site ping-pong mechanism | Rhodovulum sulfidophilum SH1 | dimethyl sulfoxide + ferrocytochrome c2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterotrimer | - |
Rhodovulum sulfidophilum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dimethyl sulfide dehydrogenase | - |
Rhodovulum sulfidophilum |
| DMS dehydrogenase | - |
Rhodovulum sulfidophilum |
| DMS:ferricytochrome c2 oxidoreductase | - |
Rhodovulum sulfidophilum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.3 | - |
- |
Rhodovulum sulfidophilum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | the enzyme contains a heme b cofactor | Rhodovulum sulfidophilum | |
| iron-sulfur centre | the enzyme contains five iron-sulfur clusters | Rhodovulum sulfidophilum | |
| molybdopterin | - |
Rhodovulum sulfidophilum | |
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Release 2023.1 (January 2023)
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