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Literature summary for 5.6.1.4 extracted from

  • Duan, D.; Hnatchuk, D.; Brenner, J.; Davis, D.; Allingham, J.
    Crystal structure of the Kar3-like kinesin motor domain from the filamentous fungus Ashbya gossypii (2012), Proteins Struct. Funct. Bioinform., 80, 1016-1027.
    View publication on PubMed
Search for more literature for 5.6.1.4

Cloned(Commentary)

Cloned (Comment) Organism
motor domain (Leu363-Arg709) expressed in Escherichia coli BL21(DE3)-RIL CodonPlus Eremothecium gossypii

Crystallization (Commentary)

Crystallization (Comment) Organism
motor domain MgADP complex, hanging drop vapor diffusion method, room temperature, 14% PEG 3350, pH 8.5 Eremothecium gossypii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0016
-
 ATP motor domain, 0 mM potassium acetate, pH 6.9, 22°C Eremothecium gossypii

Organism

Organism UniProt Comment Textmining
Eremothecium gossypii
-
 ATCC 10895
-

Purification (Commentary)

Purification (Comment) Organism
-
 Eremothecium gossypii

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
AgKar3
-
 Eremothecium gossypii
Kar3-like kinesin
-
 Eremothecium gossypii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 ATP addition of the ATP analog adenylyl-imidodiphosphate (AMPPNP, 1 mM) dramatically increases the microtuble affinity Eremothecium gossypii
0.16
-
 ATP motor domain, 25 mM potassium acetate, Vmax/2 at 0.0007 mM microtubles, pH 6.9, 22°C Eremothecium gossypii
0.17
-
 ATP motor domain, 0 mM potassium acetate, Vmax/2 at 0.00008 mM microtubles, pH 6.9, 22°C Eremothecium gossypii