title: OMP decarboxylase--An enigma persists.
abstract: In 1995, Radzicka and Wolfenden reported that the rate enhancement produced by orotidine 5'-phosphate decarboxylase (ODCase) approaches 10(17), making this enzyme the most effective pure protein catalyst known in Nature [A. Radzicka, R. Wolfenden, Science 267 (1995) 90-93]. Over the last 12 years, there have been many hypotheses put forward to explain that impressive effect. In this perspective, we provide a summary of the reaction pathways under consideration for ODCase, highlight the supporting and refuting data, and suggest experiments designed to further test each of the candidate pathways.
authors: Division of Infectious Disease, Wadsworth Center--NYS-DOH, Albany, NY 12202, USA. callahan@wadsworth.org
authors: Brian P
authors: BP
authors: Callahan
authors: Brian G
authors: BG
authors: Miller
mesh_terms: D002384:Catalysis; D009964:Orotidine-5'-Phosphate Decarboxylase / Q000378:metabolism*; D014542:Uridine Monophosphate / Q000031:analogs & derivatives* / Q000378:metabolism; D015003:Yeasts / Q000201:enzymology*
chemical_list: C005417:orotidylic acid; D014542:Uridine Monophosphate; D009964:Orotidine-5'-Phosphate Decarboxylase