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Literature summary for 5.6.1.3 extracted from

  • Adio, S.; Woehlke, G.
    Properties of the kinesin-3 NcKin3 motor domain and implications for neck function (2009), FEBS J., 276, 3641-3655.
    View publication on PubMed
Search for more literature for 5.6.1.3

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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 additional information overview, comparison of the kinetic parameters of monomeric and dimeric NcKin3 Neurospora crassa
additional information
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 additional information 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 Neurospora crassa

Organism

Organism UniProt Comment Textmining
Neurospora crassa
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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 Neurospora crassa ATP + H2O + a kinesin associated with a microtubule at position n =
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 r
ATP + H2O + a kinesin associated with a microtubule at position n
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 Neurospora crassa ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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 ?

Subunits

Subunits Comment Organism
dimer NcKin3 is dimeric but inactivates one of its motor heads to generate nonprocessive motility. The heads of the wild-type Nckin3 motor are strictly coupled via the neck domain, and the dimeric structure is required for proper detachment after one ATPase cycle Neurospora crassa

Synonyms

Synonyms Comment Organism
NcKin3 a member of the kinesin-3 family Neurospora crassa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
additional information
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 monomeric and dimeric activation energies (Arrhenius equation) 5.2 kJ/mol and 4.1 kJ/mol, respectively Neurospora crassa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
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 additional information in presence of microtubule the ATP hydrolysis is activated 3fold to 4fold compared to kcat, 125 vs. 34 s-1, while phosphate release is approximately equally fast: 29 s-1 Neurospora crassa
additional information
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 additional information steady state ATPase parameters, kcat values and gliding velocities of truncated NcKin3 constructs Neurospora crassa
29
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 phosphate in presence of microtubule the ATP hydrolysis is activated 3fold to 4fold compared to kcat, 125 vs. 34 s-1, while phosphate release is approximately equally fast: 29 s-1, pH and temperature not specified in the publication Neurospora crassa
34
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 ADP in presence of microtubule the ATP hydrolysis is activated 3fold to 4fold compared to kcat, 125 vs. 34 s-1, while phosphate release is approximately equally fast: 29 s-1, pH and temperature not specified in the publication Neurospora crassa