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Literature summary for 5.6.1.3 extracted from

  • Krzysiak, T.C.; Wendt, T.; Sproul, L.R.; Tittmann, P.; Gross, H.; Gilbert, S.P.; Hoenger, A.
    A structural model for monastrol inhibition of dimeric kinesin Eg5 (2006), EMBO J., 25, 2263-2273.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
monastrol model for dimeric Eg5 in which monastrol stabilizes a conformation with the neck linker of each motor domain locked onto its catalytic core, resulting in dissociation of the MT. Eg5 complex or an inhibition of MT binding Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0079
-
ATP dimeric Eg5-513 Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + a kinesin associated with a microtubule at position n Homo sapiens
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ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a kinesin associated with a microtubule at position n
-
Homo sapiens ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
?
ATP + H2O + a kinesin associated with a microtubule at position n Eg5 is a homotetrameric kinesin-5 involved in centrosome separation and assembly of the bipolar mitotic spindle. The stable dimer Eg5-513 promotes robust plus-end-directed microtubule gliding at a rate similar to that of homotetrameric Eg5 in vitro. Eg5-513 exhibits slow ATP turnover, high affinity for ATP, and a weakened affinity for microtubules when compared to monomeric Eg5 Homo sapiens ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
?

Subunits

Subunits Comment Organism
More Eg5 is a homotetrameric kinesin-5 involved in centrosome separation and assembly of the bipolar mitotic spindle. The stable dimer Eg5-513 promotes robust plus-end-directed microtubule gliding at a rate similar to that of homotetrameric Eg5 in vitro. Eg5-513 exhibits slow ATP turnover, high affinity for ATP, and a weakened affinity for microtubules when compared to monomeric Eg5 Homo sapiens

Synonyms

Synonyms Comment Organism
kinesin Eg5
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.48
-
ATP dimeric Eg5-513 Homo sapiens