Interrogation of the active site of OMP decarboxylase from Escherichia coli with a substrate analogue bearing an anionic group at C6

Abstract

An analogue of orotidine 5′-monophosphate (OMP), 6-phosphonouridine 5′-monophosphate is a competitive inhibitor of OMP decarboxylase from E. coli, binding with an affinity similar to that of OMP. Hence the active site is capable of stabilizing negative charge distributed out of the plane of the pyrimidine ring, consistent with the notion of ground state destabilization.