Fig. 2
From: Kinesin-3 motors are fine-tuned at the molecular level to endow distinct mechanical outputs
Kinesin-3 motors exhibit high ATPase activity and differential microtubule affinity. MT-stimulated ATPase activity of full-length and truncated constitutively active motors was measured using Sf9-purified proteins. A Comparison of ATPase activity between full-length and constitutively active kinesin motors. ATPase activity for full-length motors was measured at MT concentration that had highest ATPase activity for the respective constitutively active motor. B–F Plots showing ATPase activity against varied concentrations of MTs for B constitutively active kinesin-1 motor, KHC (1–560) and kinesin-3 motors C KIF1A(1-393LZ), D KIF13A(1-411ΔP), E KIF13B(1-412ΔP), and F KIF16B(1–400) and fit to Michaelis–Menten equation. Maximal turnover (kcat) and MT affinity (Km) parameters were determined using GraphPad Prism. Error bars represent mean ± SD. Data presented from three independent experiments