title: An unprecedented twist to ODCase catalytic activity.
abstract: Orotidine-5'-monophosphate decarboxylase (ODCase) has evolved to catalyze a decarboxylation reaction, most probably via a carbanion species at the C6 position of orotidine-5'-monophosphate. We reveal an unusual biochemical pathway of conversion of 6-cyano-uridine-5'-monophosphate by ODCase to barbiturate-5'-monophosphate via perhaps an electrophilic center at the C6 position, leading to inhibition. This potential of ODCase is very useful in the design of novel inhibitors.
authors.affiliation: Molecular Design and Information Technology Center, Leslie Dan Faculty of Pharmacy, Toronto, ON M5S 2S2 Canada.
authors.forename: Masahiro
authors.initials: M
authors.lastname: Fujihashi
authors.forename: Angelica M
authors.initials: AM
authors.lastname: Bello
authors.forename: Ewa
authors.initials: E
authors.lastname: Poduch
authors.forename: Lianhu
authors.initials: L
authors.lastname: Wei
authors.forename: Subhash C
authors.initials: SC
authors.lastname: Annedi
authors.forename: Emil F
authors.initials: EF
authors.lastname: Pai
authors.forename: Lakshmi P
authors.initials: LP
authors.lastname: Kotra
mesh_terms: D002384:Catalysis; D018360:Crystallography, X-Ray; D013058:Mass Spectrometry; D017014:Methanobacterium / Q000201:enzymology; D009955:Ornithine Decarboxylase / Q000737:chemistry* / Q000378:metabolism*; D055672:Static Electricity; D013997:Time Factors
chemical_list: D009955:Ornithine Decarboxylase