| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1356214 | Bioorganic Chemistry | 2007 | 5 Pages |
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.
Graphical abstract■■■Figure optionsDownload full-size imageDownload as PowerPoint slide
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Brian P. Callahan, Brian G. Miller,