Kinetic Isotope Effects in the Active Site of B-Subtilis Chorismate Mutase
S. E. Worthington, A. E. Roitberg, Morris Krauss
Kinetic Isotope Effects are determined for the enzyme-catalyzed Claisen rearrangement of chorismate to prephenate using computational methods. The reported kinetic isotope effects compare reasonably well with the few available experimental values. The relative trends observed for the computed and the measured kinetic isotope effects are in excellent agreement. We report the kinetic isotope effects for all the atoms of substrate with the exception of the carboxylate groups. Although the absolute values may differ when determined experimentally, the relative trends noted for the computed kinetic isotope effects should be accurate when the experimental data becomes available.
International Journal of Quantum Chemistry
ab initio reaction path, active site activation of reactant, chorismate mutase, effect, effective fragment potentials, kinetic isotope