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. Author manuscript; available in PMC: 2009 Dec 1.
Published in final edited form as: Arch Biochem Biophys. 2008 Sep 18;480(1):58–67. doi: 10.1016/j.abb.2008.08.024

Figure 6.

Figure 6

Competition for the mevalonate diphosphate site of wild-type human MDD. Double-reciprocal plots of the reaction velocity as a function of mevalonate 5-diphosphate concentration, measured at different levels of the inhibitors diphosphoglycolyl proline (A) or 6-fluoromevalonate 5-diphosphate (B). Data were fit to a competitive inhibition model using SigmaPlot 10.0/Enzyme Kinetics 1.3. (Systat Software, Inc.). Panel (A) displays the inhibition by diphosphoglycolyl proline measured at the following concentrations: (●) 0.0 mM, (○) 2.7μM, (▼) 5.5 μM, (▽) 11.0 μM, (■) 16.5 μM. Panel (B) displays the inhibition by 6-fluoromevalonate 5-diphosphate measured at the following concentrations: (●) 0.0 nM, (○) 32 nM, (▼) 65 nM, (▽) 194 nM, (■) 484 nM.