Abstract
In 1995, Radzicka and Wolfenden reported that the rate enhancement produced by orotidine 5′-phosphate decarboxylase (ODCase) approaches 1017, 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.
| Original language | English |
|---|---|
| Pages (from-to) | 465-469 |
| Number of pages | 5 |
| Journal | Bioorganic Chemistry |
| Volume | 35 |
| Issue number | 6 |
| DOIs | |
| State | Published - Dec 2007 |
Keywords
- Carbanion
- Carbene
- Decarboxylase
- Decarboxylation
- Electrostatic stress
- Mechanism
- OMP
- Orotidine
- Transition state
- Ylide
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