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. 2014 Apr 15;289(23):16601–16614. doi: 10.1074/jbc.M114.551408

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© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 5. — Double-reciprocal plot analysis of selective inhibitor MMV666693. A, double-reciprocal plot analysis of PvEg5 to determine the mode of inhibition with respect to ATP. We find that both K_m and V_max vary at different inhibitor concentrations, supporting an allosteric mixed mode model of inhibition. K_m values are 33 ± 5, 66 ± 26, and 110 ± 75 for 0, 25, and 75 μm inhibitor, respectively. V_max values are 0.22 ± 0.02, 0.19 ± 0.07, and 0.11 ± 0.08 for 0, 25, and 75 μm inhibitor, respectively. B, double-reciprocal plot analysis of PvEg5 to determine the mode of inhibition with respect to microtubules. Similar to the results with ATP, we find that both K_m and V_max vary at different inhibitor concentrations, again supporting an allosteric mixed mode model of inhibition. K_m values are 0.03 ± 0.01, 0.20 ± 0.07, and 0.40 ± 0.13 for 0, 25, and 75 μm inhibitor, respectively. V_max values are 1.5 ± 0.1, 1.0 ± 0.3, and 0.3 ± 0.1 for 0, 25, and 75 μm inhibitor, respectively.