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Results 1 - 5 of 5
EC Number Reaction Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.4ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end) a molecular mechanical model for the Kar3/Vik1 heterodimer is described based on structural, kinetic and motility data revealing a long-range chemomechanical transmission mechanism that resembles a familiar fishing tactic. By this this molecular fishing, ATP-binding to Kar3 dissociates catalytically inactive Vik1 off microtubule to facilitate minus-end sliding of the dimer on the microtubule lattice. When the dimer binds the frayed ends of the microtubules, the fishing channels ATP hydrolysis energy into the microtubule depolymerization by a mechanochemical effect 713213
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.4ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end) kinetics, comparison of wild-type enzyme and enzyme with N-terminal glutathione S-transferase tag, mechanism 656259
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.4ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end) mechanism, model of movement 655330
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.4ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end) model for enzymic coupling of depolymerizing microtubule plus ends to the cell cortex 655282
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.4ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end) structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules 210546, 210548, 210551, 210557, 210558, 210559, 210560, 210561, 210562, 210563, 210565, 210567, 210568, 210569, 210570, 210571, 210572, 210574
Results 1 - 5 of 5