Activating Compound | Comment | Organism | Structure |
---|---|---|---|
microtubule | concentration for half-maximal stimulation of wild-type 0.0009 mM. Analysis of stimulation for mutants G272C, S275C, A247C, L249C, A252C in native form and modified with 4-phenylazophenyl maleimid | Mus musculus |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
A247C | mutation in loop L11. Mutant retains normal enzymatic properties | Mus musculus |
L249C | mutation in loop L11. Vmax value is reduced by 20%. After modification by 4-phenylazophenyl maleimide, mutant exhibits reversible alterations in ATPase activity accompanied by cis-trans isomerization upon UV and VIS light irradiation. The APTase activity exhibited by the cis-isomer of the 4-phenylazophenyl maleimide bound to the mutant is half of that of the trans-isomer | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + a kinesin associated with a microtubule at position n | - |
Mus musculus | ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end) | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.004 | - |
ATP | mutant A247C, pH 6.7, 25°C | Mus musculus | |
0.005 | - |
ATP | mutant G272C, pH 6.7, 25°C | Mus musculus | |
0.014 | - |
ATP | mutant A252C, pH 6.7, 25°C | Mus musculus | |
0.021 | - |
ATP | mutant L249C, pH 6.7, 25°C | Mus musculus | |
0.023 | - |
ATP | mutant S275C, pH 6.7, 25°C | Mus musculus | |
0.023 | - |
ATP | wild-type, pH 6.7, 25°C | Mus musculus |