Bioorg Chem. 2007 Dec;35(6):465-9. Epub 2007 Sep 21.

OMP decarboxylase--An enigma persists.

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Division of Infectious Disease, Wadsworth Center--NYS-DOH, Albany, NY 12202, USA. callahan@wadsworth.org

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.

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Cited by 5 PubMed Central articles

Determination of the amino acid sequence requirements for catalysis by the highly proficient orotidine monophosphate decarboxylase. [Protein Sci. 2011]
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OMP decarboxylase: phosphodianion binding energy is used to stabilize a vinyl carbanion intermediate. [J Am Chem Soc. 2011]
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Goryanova B, Amyes TL, Gerlt JA, Richard JP. J Am Chem Soc. 2011 May 4; 133(17):6545-8. Epub 2011 Apr 12.
Product deuterium isotope effects for orotidine 5'-monophosphate decarboxylase: effect of changing substrate and enzyme structure on the partitioning of the vinyl carbanion reaction intermediate. [J Am Chem Soc. 2010]
Product deuterium isotope effects for orotidine 5'-monophosphate decarboxylase: effect of changing substrate and enzyme structure on the partitioning of the vinyl carbanion reaction intermediate.
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OMP decarboxylase--An enigma persists.
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