Interacting head mechanism of microtubule-kinesin ATPase.

  title={Interacting head mechanism of microtubule-kinesin ATPase.},
  author={Y. Zee Ma and Edwin W. Taylor},
  journal={The Journal of biological chemistry},
  volume={272 2},
Kinetic and equilibrium properties are compared for a monomeric kinesin construct (K332) and a dimeric construct (K379). MtK379 has a low affinity (5 x 10(4) M(-1)) and a high affinity (5 x 10(6) M(-1)) binding site for mant ADP while MtK332 has a single low affinity site (5 x 10(4) M(-1)). Rate constants of dissociation of mant ADP are <1 s(-1) for the high affinity site and 75-100 s(-1) for the low affinity site for MtK379. For MtK332, the effective rate constant is 200-300 s(-1). It is… CONTINUE READING
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