TABLE 2.

Basal and MT-stimulated ATPase rates for wild type and modified kinesin-5 motor domains

Data are the average values for three replicates obtained from three independent enzyme preparations. S.E. are also reported. Klp61F-WT exhibited a higher basal and MT-stimulated ATPase rate than the chimeras (unpaired t test, p < 0.001), whereas the -fold increase upon MT stimulation was indistinguishable among the Klp61F constructs (15-fold, unpaired t test, p < 0.05).

Motor domain	Rate of ATP hydrolysis
	Basal	MT-stimulated
	ADP motor−1s−1
HsEg5	0.17 ± 0.05	7.69 ± 0.17
Klp61F-WT	0.05 ± 0.01	0.66 ± 0.02
Klp61F-L5	0.04 ± 0.01	0.51 ± 0.02
Klp61F-L5-α3	0.04 ± 0.01	0.53 ± 0.02