Journal
ACCOUNTS OF CHEMICAL RESEARCH
Volume 35, Issue 4, Pages 237-246Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ar000056y
Keywords
-
Categories
Ask authors/readers for more resources
Epimerases and racemases are enzymes that catalyze the inversion of stereochemistry in biological molecules. In this article, three distinct examples are used to illustrate the wide range of chemical strategies employed during catalysis, and the diverse set of ancestors from which these enzymes have evolved. Glutamate racemase is an example of an enzyme that operates at an activated stereocenter (bearing a relatively acidic proton) and employs a nonstereospecific deprotonation/reprotonation mechanism. UDP-N-Acetylglucosamine 2-epimerase acts at an unactivated stereocenter and uses a mechanism involving a nonstereospecific elimination/addition of UDP. L-Ribulose phosphate 4-epimerase also acts at an unactivated stereocenter and uses a nonstereospecific retroaldol/aldol mechanism.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available