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. Author manuscript; available in PMC: 2013 Oct 2.
Published in final edited form as: Biochemistry. 2012 Sep 19;51(39):7733–7739. doi: 10.1021/bi3009054

Figure 5.

Figure 5

Enzyme kinetic plots of initial velocity/[E] vs. substrate concentration demonstrating a solvent kinetic isotope effect. Tryptophan is the variable substrate and saturating DMAPP (20 μM) was employed. Triangles represent data obtained in H2O and squares represent data obtained in > 95% D2O. Data was fit to the Michaelis-Menten equation (dashed line = H2O and solid line = D2O).