title: 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.
authors.affiliation: Department of Biochemistry & Molecular Biology, Dalhousie University, Halifax, Nova Scotia, B3H 1X5, Canada.
authors.forename: Srinath
authors.initials: S
authors.lastname: Thirumalairajan
authors.forename: Brandi
authors.initials: B
authors.lastname: Mahaney
authors.forename: Stephen L
authors.initials: SL
authors.lastname: Bearne
mesh_terms: D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology*; D009964:Orotidine-5'-Phosphate Decarboxylase / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D009964:Orotidine-5'-Phosphate Decarboxylase