Remarkable rate enhancement of orotidine 5'-monophosphate decarboxylase is due to transition-state stabilization rather than to ground-state destabilization

Results show that the ground-state destabilization does not play a role in enzyme catalysis as shown by the rate enhancement measurements of orotidine 5'-phosphate decarboxylase (ODCase). Data reveal that electrostatic effects are involved in the catalysis reactions which, in turn are associated with transition state stabilization.