EC Number   |
Metals/Ions |
Reference |
|---|
   2.5.1.59 | Cd2+ |
80% of maximal activity in the presence of 0.5 mM alone |
636539 |
| 2.5.1.59 | Cd2+ |
Cd-substituted enzyme has altered specificities with regard to utilization of both peptide and isoprenoid substrates |
636541 |
| 2.5.1.59 | Cd2+ |
the zinc in enzyme can be replaced by Cd2+ |
636537, 636539, 636541 |
| 2.5.1.59 | Mg2+ |
20% of maximal activity in the presence of 0.5 mM alone |
636539 |
| 2.5.1.59 | Mg2+ |
for maximum reaction rate |
687774 |
| 2.5.1.59 | Mg2+ |
no requirement |
636537, 636541 |
| 2.5.1.59 | Mg2+ |
prenylation rate constant of wild type enzyme is not dependent on Mg2+ and is about 20fold slower than the maximal rate constant catalyzed by protein farnesyltransferase. Prenylation rate constant in mutant Kbeta311A or Kbeta311D decreases in absence of magnesium 941fold without significantly affecting the binding affinityof either substrate. Furthermore, the geranylgeranylation rate constant is enhanced by the addition of Mg2+ for Kbeta311A and Kbeta311D GGTase I 25-fold compared with wild type GGTase I. These results demonstrate that lysine beta311 of GGTase I partially replaces the catalytic function of Mg2+ observed in protein farnesyltransferase |
659363 |
| 2.5.1.59 | Mg2+ |
required, optimal activity of EDTA-treated enzyme at 0.5 mM, Mg2+ probably activates the diphosphate leaving group of enzyme, and is essential for transferring the bound peptide substrate |
636545 |
| 2.5.1.59 | Mg2+ |
requirement, optimal activity at 0.5 mM in presence of 0.1 mM Zn2+ |
636543 |
| 2.5.1.59 | Mn2+ |
60% of maximal activity in the presence of 0.5 mM alone |
636539 |
