EC Number   |
Natural Substrates |
|---|
   5.6.1.3 | more |
KLP61F displays a 3fold higher preference for crosslinking microtubules in the antiparallel orientation, this polarity preference is observed in the presence of ADP or ATP plus AMPPNP, but not AMPPNP alone |
| 5.6.1.3 | more |
NOD binds tightly to microtubules in the nucleotide-free state, yet other nucleotide states, including adenosine-5'-(beta,gamma-imido)triphosphate, are weakened, NOD interaction with microtubules occurs slowly with weak activation of ADP product release. Upon rapid substrate binding, NOD detaches from the microtubule prior to the rate-limiting step of ATP hydrolysis. |
| 5.6.1.3 | more |
the binding of tail peptides to head dimers is fast and readily reversible, the second tail peptide in a folded kinesin-1 may be available to bind other molecules while kinesin-1 remains folded |
| 5.6.1.3 | more |
enzyme TbKIN-D associates with cytoskeletal microtubules in vivo, and TbKIN-D interacts with TbKIN-C, a kinetoplastid-specific kinesin |
| 5.6.1.3 | more |
KIF4 specifically binds to the microtubule, enzyme interaction with tubulin, the KIF4-specific Q248 and K249 form possible hydrogen bonds with Y108 of helix H3' of alpha-tubulin. Microtubule filament binding by enzyme KIF4, around the center line of the microtubule protofilament, the helix-alpha4-mediated microtubule-binding site is located and fitted into the intra-tubulin dimer groove |
| 5.6.1.3 | more |
the KVD motif of kinesin Kif2C interacts directly with tubulin. ATP hydrolysis in Kif2C is not required for tubulin release |
