EC Number   |
Metals/Ions |
Reference |
|---|
   2.5.1.58 | Cd2+ |
substitution of the active site zinc with cadmium increases the affinity of the peptide substrate and decreases the rate constant for the chemical step |
637513 |
| 2.5.1.58 | Co2+ |
- |
637504 |
| 2.5.1.58 | Co2+ |
evidence for a catalytically relevant interaction between the metal ion and the protein substrate in the enzyme |
637505 |
| 2.5.1.58 | Mg2+ |
10 mM, required |
673089 |
| 2.5.1.58 | Mg2+ |
appears to coordinate the diphosphate moiety of farnesyl diphosphate |
637502, 637513, 637514 |
| 2.5.1.58 | Mg2+ |
enhances activity several hundred-fold, with a Km(Mg2+) value of 4 mM. Mg2+ coordinates the side chain carboxylate of Asp-beta352 and that the role of magnesium in the reaction includes positioning the FPP prior to catalysis. Mg2+ may accelerate catalysis both by stabilizing developing negative charge in the transition state and by stabilizing the active site conformation prior to catalysis |
659292 |
| 2.5.1.58 | Mg2+ |
magnesium is not required for formation of the thioether product but the presence increases the single-turnover rate constant by several orders of magnitude at saturating enzyme and substrate concentrations |
637513 |
| 2.5.1.58 | Mg2+ |
required |
636537, 637502, 637503, 637507, 637508, 637516, 637518, 637520, 685102, 738097, 738158, 739602 |
| 2.5.1.58 | Mg2+ |
required for activity |
687188 |
| 2.5.1.58 | Mg2+ |
required, stabilizes the developing negative charge on the diphosphate as the bond breaks between the a-phosphate and the C1 atom of the farnesyl group |
675272 |
