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. Author manuscript; available in PMC: 2014 Jun 21.
Published in final edited form as: ACS Chem Biol. 2013 Mar 29;8(6):1232–1240. doi: 10.1021/cb400027q

Figure 5. Effect of the active site R465A mutation on the binding of αKG and PEP to EIC.

Figure 5

(a) Binding of αKG to the R465A EIC mutant as monitored by chemical shift perturbation. Data for all residues showing ΔH/N > 0.1 ppm at 16 mM αKG were simultaneously fit (solid curve) using a one-site binding model (see Methods). In the figure, the ΔH/N were normalized with respect to the fitted ΔH/N at saturation and averaged over all the residues used in the fitting procedure. (b) Michaelis-Menten kinetics for the R465A EIC mutant with the substrate PEP in the absence of αKG. The error bars are set to one standard deviation.