EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   5.6.1.3 | -999 |
- |
more |
Michaelis-Menten kinetics, and steady-state ATPase activities of three types of chimeric construct, overview |
734474 |
| 5.6.1.3 | -999 |
- |
more |
microtubule-activated ATPase kinetics of wild-type and mutant enzymes |
734238 |
| 5.6.1.3 | -999 |
- |
more |
modeling reveals allosterically coupled motions driving the APO to ATP transition of ATPase states, binding free energy analysis |
733362 |
| 5.6.1.3 | -999 |
- |
more |
overview, comparison of the kinetic parameters of monomeric and dimeric NcKin3 |
711973 |
| 5.6.1.3 | -999 |
- |
more |
steady state and transient kinetics studies of fluorescence-labeled W127C mutant |
734241 |
| 5.6.1.3 | -999 |
- |
more |
the kinetic analysis suggests futile ATP hydrolysis cycles, because a representative monomer shows a faster ATP turnover than the dimer while supporting slower motility. The K0.5MT (microtubule) is 70fold lower, the microtubule-bound portion of the kinetic cycle 8fold longer and the microtubule detachment rate almost 15fold slower than the dimer |
711973 |
| 5.6.1.3 | 0.000047 |
- |
ATP |
pH 6.8, 25°C, tubuline-stimulated recombinant Kif2C functional domain mutant DSK |
734310 |
| 5.6.1.3 | 0.000058 |
- |
ATP |
pH 6.8, 25°C, tubuline-stimulated recombinant Kif2C functional domain mutant DVK |
734310 |
| 5.6.1.3 | 0.00008 |
- |
ATP |
pH 6.8, 25°C, tubulin-stimulated recombinant Kif2C functional domain wild-type |
734310 |
| 5.6.1.3 | 0.00018 |
- |
ATP |
pH 6.8, 25°C, tubulin-stimulated recombinant Kif2C functional domain mutant L2 |
734310 |
