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Literature summary for 5.6.1.4 extracted from

  • Mackey, A.T.; Sproul, L.R.; Sontag, C.A.; Satterwhite, L.L.; Correia, J.J.; Gilbert, S.P.
    Mechanistic analysis of the Saccharomyces cerevisiae kinesin Kar3 (2004), J. Biol. Chem., 279, 51354-51361.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.4

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information ATP-binding is significantly faster for enzyme-GST fusion protein than for wild-type enzyme Saccharomyces cerevisiae
0.012
-
 ATP both wild-type and GST-fusion protein, pH 7.2, 25°C Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 comparison of wild-type enzyme and enzyme fused with N-terminal glutathione S-transferase
-

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end) kinetics, comparison of wild-type enzyme and enzyme with N-terminal glutathione S-transferase tag, mechanism Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a kinesin associated with a microtubule at position n
-
 Saccharomyces cerevisiae ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
 ?

Synonyms

Synonyms Comment Organism
Kar3
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
70
-
 ATP both wild-type and GST-fusion protein, pH 7.2, 25°C Saccharomyces cerevisiae