EC Number   |
Metals/Ions |
Reference |
|---|
    2.5.1.29 | Ca2+ |
about 10% of the activity with Mg2+ |
726880 |
| 2.5.1.29 | Ca2+ |
the enzyme requires Mg2+ and is inactive in the absence of metal. Optimal concentration of Mg2+ is 0.1 mM. Co2+ and Mn2+ activate the synthesis of farnesyl diphosphat at lower concentrations (0.005-0.05 mM) than does Mg2+ (0.05-0.5 mM). The enzyme also utilizes Ca2+, Ni2+, and Zn2+ as cofactors, but only at low concentrations (0.001-0.05 mM) |
758863 |
| 2.5.1.29 | Co2+ |
activates, less effective than Mg2+ |
638741 |
| 2.5.1.29 | Co2+ |
the enzyme requires Mg2+ and is inactive in the absence of metal. Optimal concentration of Mg2+ is 0.1 mM. Co2+ and Mn2+ activate the synthesis of farnesyl diphosphat at lower concentrations (0.005-0.05 mM) than does Mg2+ (0.05-0.5 mM). The enzyme also utilizes Ca2+, Ni2+, and Zn2+ as cofactors, but only at low concentrations (0.001-0.05 mM) |
758863 |
| 2.5.1.29 | Cu2+ |
about 5% of the activity with Mg2+ |
726880 |
| 2.5.1.29 | KCl |
200-2300 mM, enhances activity approx. 10fold |
638745 |
| 2.5.1.29 | KCl |
800 mM, activates |
638744 |
| 2.5.1.29 | Mg2+ |
- |
671788, 673666, 674562, 674614, 676609, 676706 |
| 2.5.1.29 | Mg2+ |
bisphosphonate binding depends on coordination by Mg2+. Three Mg2+ ions are involved in bisphosphonate-protein interactions. Mg2+ ions are vital for drug binding and provide a structural basis for future computational design of geranylgeranyl diphosphate inhibitors |
759790 |
| 2.5.1.29 | Mg2+ |
less effective than Mn2+ |
638739, 638741, 638750 |
