EC Number   |
Metals/Ions |
Reference |
|---|
    2.5.1.30 | Mg2+ |
absolute requirement |
637624 |
| 2.5.1.30 | Mg2+ |
required for activity |
759075 |
| 2.5.1.30 | Mg2+ |
required, no activation with Mn2+ |
637623 |
| 2.5.1.30 | Mg2+ |
requires a divalent cation for the enzymatic activity with an optimal level of 1 mM Mg2+ or 2 mM Mn2+, respectively |
637627 |
| 2.5.1.30 | Mg2+ |
this enzyme is composed of two dissociable subunits that exhibit a catalytic activity only when they are associated together in the presence of a cofactor, Mg2+, and a substrate, farnesyl diphosphate. The quartz-crystal microbalance measurement reveals that farnesyl diphosphate is preferentially bound to subunit II in the presence of Mg2+, while the atomic force microscopy measurement shows that the adhesive force between the subunits is observed only in the presence of both Mg2+ and farnesyl diphosphate |
674185 |
| 2.5.1.30 | Mn2+ |
30% of the activation obtained with Mg2+ |
637624 |
| 2.5.1.30 | Mn2+ |
requires a divalent cation for the enzymatic activity with an optimal level of 1 mM Mg2+ or 2 mM Mn2+, respectively |
637627 |
