TABLE 1
Comparison of substrate affinity in WT PDE11 versus the Q869A mutant
Values are given as mean ± S.E.M. The Michaelis-Menten constant (Km) for cAMP and cGMP and calculation of the loss of free energy of binding (ΔΔG) were determined as described under Materials and Methods. ΔΔG values were calculated from the Km and not independently measured. -Fold change was calculated by dividing the Q869A value by that for WT PDE11A4. Results are derived from results from at least three experiments in which each was assayed in triplicate.