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Literature summary for 1.8.1.5 extracted from
- Mechanism of inhibition of aliphatic epoxide carboxylation by the coenzyme M analog 2-bromoethanesulfonate (2010), J. Biol. Chem., 285, 25232-25242.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-bromoethanesulfonate | reversible inhibitor, time-dependent inactivator of dithiothreitol-reduced 2-ketopropyl-CoM carboxylase/oxidoreductase, where the redox active cysteines are in the free thiol forms, does not inactivate air-oxidized 2-ketopropyl-CoM carboxylase/oxidoreductase, where the redox active cysteine pair is in the disulfide form. Inactivation leads to covalent modification of the interchange thiol residue C82. The flavin thiol Cys87 is not alkylated by 2-bromoethanesulfonate under reducing conditions, and no amino acid residues are modified by 2-bromoethanesulfonate in the oxidized enzyme | Xanthobacter autotrophicus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Xanthobacter autotrophicus | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 2-KPCC | - |
Xanthobacter autotrophicus |
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Release 2023.1 (January 2023)
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