EC Number   |
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Reference |
|---|
   5.6.1.3 | -999 |
- |
more |
in presence of microtubule the ATP hydrolysis is activated 3fold to 4fold compared to kcat, 125 vs. 34 s-1, while phosphate release is approximately equally fast: 29 s-1 |
711973 |
| 5.6.1.3 | -999 |
- |
more |
steady state ATPase parameters, kcat values and gliding velocities of truncated NcKin3 constructs |
711973 |
| 5.6.1.3 | 0.0009 |
- |
methylanthraniloyl-ATP |
basal activity, in absence of tubulin or microtubles, pH 6.9, 25°C |
719368 |
| 5.6.1.3 | 0.00095 |
- |
ATP |
basal activity, in absence of tubulin or microtubles, pH 6.9, 25°C |
719368 |
| 5.6.1.3 | 0.004 |
- |
ATP |
mutant A247C, pH 6.7, 25°C |
687450 |
| 5.6.1.3 | 0.005 |
- |
ATP |
mutant G272C, pH 6.7, 25°C |
687450 |
| 5.6.1.3 | 0.014 |
- |
ATP |
mutant A252C, pH 6.7, 25°C |
687450 |
| 5.6.1.3 | 0.021 |
- |
ATP |
mutant L249C, pH 6.7, 25°C |
687450 |
| 5.6.1.3 | 0.023 |
- |
ATP |
mutant S275C, pH 6.7, 25°C |
687450 |
| 5.6.1.3 | 0.023 |
- |
ATP |
wild-type, pH 6.7, 25°C |
687450 |
