EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.8.2.1 | periplasm | - |
Sinorhizobium meliloti | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.8.2.1 | Mo4+ | molybdenum enzyme. Sulfite oxidizing enzymes (regardless of origin) share a common active site comprising a dioxido-MoVI moiety chelated by a molybdopterin dithiolene ligand in addition to a cysteinyl S-donor. The equatorial oxido ligand is the one transferred to sulfite during its 2-electron O-atom transfer reaction | Sinorhizobium meliloti | |
1.8.2.1 | additional information | the enzyme bears no heme cofactor | Sinorhizobium meliloti |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.8.2.1 | 78000 | - |
- |
Sinorhizobium meliloti |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.2.1 | sulfite + 2 ferricytochrome c + H2O | Sinorhizobium meliloti | - |
sulfate + 2 ferrocytochrome c + 2 H+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.2.1 | Sinorhizobium meliloti | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.8.2.1 | sulfite + 2 ferricytochrome c + H2O = sulfate + 2 ferrocytochrome c + 2 H+ | mechanism of electrochemically mediated, enzyme SorT-catalyzed sulfite oxidation | Sinorhizobium meliloti |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.8.2.1 | 7.4 | - |
pH 8.0, 22°C, with horse heart cytochrome c | Sinorhizobium meliloti |
1.8.2.1 | 33.4 | - |
pH 8.0, 22°C, with SorU | Sinorhizobium meliloti |
1.8.2.1 | 470 | - |
pH 8.0, 22°C, with ferricyanide | Sinorhizobium meliloti |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.2.1 | additional information | favorable protein-protein interactions between SorT and c-type cytochrome SorU, i.e. Smc04048, lead to productive electron transfer and catalytic activity. No activity with ferrous horse heart cytochrome c, and no activity with O2 as an sulfite oxidase | Sinorhizobium meliloti | ? | - |
? | |
1.8.2.1 | sulfite + 2 ferricytochrome c + H2O | - |
Sinorhizobium meliloti | sulfate + 2 ferrocytochrome c + 2 H+ | - |
? | |
1.8.2.1 | sulfite + 2 ferrocene methanol + H2O | - |
Sinorhizobium meliloti | sulfate + 2 reduced ferrocene methanol + 2 H+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.8.2.1 | homodimer | - |
Sinorhizobium meliloti |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.8.2.1 | SorT | - |
Sinorhizobium meliloti |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.8.2.1 | 22 | - |
assay at room temperature | Sinorhizobium meliloti |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.8.2.1 | 22 | - |
20 min, inactivation | Sinorhizobium meliloti |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.8.2.1 | additional information | - |
the lack of a plateau prevents the determination of a genuine pH optimum, an apparently linear decrease in activity as a function of pH is not interpretable by standard models of pH-dependent enzyme activity which predict sigmoidal or bell-shaped profiles | Sinorhizobium meliloti |
1.8.2.1 | 8 | - |
assay at | Sinorhizobium meliloti |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.8.2.1 | 6 | 11 | the greatest loss in activity occurs while the enzyme is at pH 10, while in the range above pH 6 and below pH 9 there is no significant variation, inactivation at pH 11.0 | Sinorhizobium meliloti |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
1.8.2.1 | 11 | - |
irreversible time-dependent loss of catalytic activity | Sinorhizobium meliloti |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.8.2.1 | cytochrome c | c-type cytochrome SorU, i.e. Smc04048 | Sinorhizobium meliloti | |
1.8.2.1 | additional information | ferrocene methanol (in its oxidized ferrocenium form) is utilized as an artificial electron acceptor for the catalytic SorT sulfite oxidation reaction | Sinorhizobium meliloti |