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John A. Gerlt Professor of Biochemistry, Chemistry, and Biophysics Ph.D. 1974, Harvard University Mechanisms of enzyme-catalyzed reactions and functional genomics: the importance of chemistry in the evolution of new enzymatic activities John A. Gerlt 301A RAL, MC-712 600 S. Mathews Urbana IL 61801 217-244-7414 j-gerlt@uiuc.edu

We are studying three groups of enzymes that are derived from common ancestors. The members of two groups, the enolase and crotonase (enoyl CoA hydratase) superfamilies, catalyze different overall reactions that involve the formation of enolate anion intermediates that are stabilized by the active site. In the enolase superfamily these are generated by abstraction of the Éø-proton of a carboxylate anion; in the crotonase superfamily these are generated by several mechanisms, including abstraction of the Éø-proton of a coenzyme A thioester. The members of the third group, the orotidine 5’-monophosphate (OMP) decarboxylase suprafamily, catalyze different reactions that do not share any chemical attributes.