EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
5.6.1.4 | -999 |
- |
more |
ATP-binding is significantly faster for enzyme-GST fusion protein than for wild-type enzyme |
656259 |
5.6.1.4 | -999 |
- |
more |
pulse-chase kinetics of ATP binding of the nucleotide-free microtubule-Kar3Vik1 complex and acid quench kinetics of ATP hydrolysis, ATP-promoted dissociation kinetics of the microtubule-Kar3Vik1 complex, detailed overview |
734196 |
5.6.1.4 | 0.00014 |
- |
ATP |
mutants Ncd670 and Ncd700SG, pH 7.2, 25°C, microtubule-stimulated ATPase activity |
719508 |
5.6.1.4 | 0.00022 |
- |
ATP |
wild-type Ncd, pH 7.2, 25°C, microtubule-stimulated ATPase activity |
719508 |
5.6.1.4 | 0.00026 |
- |
ATP |
mutant Ncd679, pH 7.2, 25°C, microtubule-stimulated ATPase activity |
719508 |
5.6.1.4 | 0.00061 |
- |
ATP |
mutant NcdM672N, pH 7.2, 25°C, microtubule-stimulated ATPase activity |
719508 |
5.6.1.4 | 0.0016 |
- |
ATP |
motor domain, 0 mM potassium acetate, pH 6.9, 22°C |
721005 |
5.6.1.4 | 0.012 |
- |
ATP |
both wild-type and GST-fusion protein, pH 7.2, 25°C |
656259 |
5.6.1.4 | 0.0271 |
- |
ATP |
in presence of microtubles, Vmax/2 at 0.0004 mM microtubles, pH 7.2, 25°C |
719954 |
5.6.1.4 | 0.0278 |
- |
ATP |
- |
210575 |