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Literature summary for 5.6.1.3 extracted from

  • Yamada, M.D.; Nakajima, Y.; Maeda, H.; Maruta, S.
    Photocontrol of kinesin ATPase activity using an azobenzene derivative (2007), J. Biochem., 142, 691-698.
    View publication on PubMed

Activating Compound

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(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Mus musculus

Protein Variants

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

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Substrates and Products (Substrate)

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)
-
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Turnover Number [1/s]

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