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. 2017 Mar 22;292(19):7971–7983. doi: 10.1074/jbc.M117.776179

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© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.

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Figure 7. — Comparisons of catalytic efficiency by IDH1 with mutations at residue 132. The observed rate constants (k_obs) were calculated from the linear range of the slopes of plots of concentration versus time, and then fit to a hyperbolic equation to generate k_cat and K_m values. All experiments were performed at 37 °C. These catalytic parameters result from fits of kinetic data resulting from two different enzyme preparations to ensure reproducibility. A, relative catalytic efficiencies (k_cat/K_m) of the conversion of ICT to αKG using K_m values for ICT are plotted against relative hydrophobicity (43). B, relative catalytic efficiencies (k_cat/K_m) of the conversion of ICT to αKG using K_m values for ICT are plotted against van der Waals volume (44). C, relative catalytic efficiencies (k_cat/K_m) of the conversion of αKG to D2HG using K_m values for αKG are plotted against relative hydrophobicity (43). D, relative catalytic efficiencies (k_cat/K_m) of the conversion of αKG to D2HG using K_m values for αKG are plotted against van der Waals volume (44).