EC Number   |
Protein Variants |
Reference |
|---|
   2.5.1.58 | C309A |
lower kcat than the wild-type enzyme |
637505 |
| 2.5.1.58 | D109N |
loss of affinity of the enzyme for its protein substrate |
637505 |
| 2.5.1.58 | D200N |
decrease of protein substrate affinity without affecting the affinity for farnesyl diphosphate substrates |
637505 |
| 2.5.1.58 | D297A |
beta-subunit, 200fold decrease in kcat |
637512 |
| 2.5.1.58 | D297N |
beta-subunit, 200fold decrease in kcat |
637512 |
| 2.5.1.58 | D307A |
lower kcat than the wild-type enzyme |
637505 |
| 2.5.1.58 | D352A |
in the D352A mutant of the beta subunit Mg2+ binding motif, three water molecules and one oxygen atom from the alpha- and beta-phosphates of farnesyl diphosphate complete the octahedral coordination sphere of Mg2+. The absence of D352beta makes the transition of the substrates towards a conformational change harder |
722460 |
| 2.5.1.58 | Dbeta352A |
drastically alters the Mg2+-dependence of FTase catalysis without dramatically affecting the rate constant of farnesylation minus magnesium or the binding affinity of either substrate. The Km(Mg2+) increases 28-fold to 110 mM, and the farnesylation rate constant at saturating Mg2+ decreases 27-fold to 0.30 per s |
659292 |
| 2.5.1.58 | Dbeta352K |
drastically alters the Mg2+-dependence of FTase catalysis without dramatically affecting the rate constant of farnesylation minus magnesium or the binding affinity of either substrate. Mutation removes the magnesium activation of farnesylation catalyzed by FTase but does not significantly enhance the rate constant for farnesylation in the absence of Mg2+ |
659292 |
| 2.5.1.58 | E256A |
130fold higher Km for the farnesyl diphosphate substrate |
637505 |
