Abstract

This chapter presents a survey of covalent, ionic, and radical intermediates in enzyme-catalyzed reactions. In addition to covalently attached intermediates, many enzymes form tight complexes with covalent reaction intermediates, while others mediate free radical reactions. Covalent catalysis is necessary in most of the enzyme processes. These covalent intermediates facilitate catalysis by providing (1) a mechanism for preserving the group transfer potential in multistep reaction schemes, (2) a means for converting an atom or group of atoms into a better leaving group in nucleophilic reactions, (3) a physical way for transferring a reactant between topologically distant active sites on multifunctional enzymes, and (4) a capacity for creating timers, latches, and clamps. The chapter presents nearly 300 such reactions in a tabular form and, where possible, includes Enzyme Commission classification numbers.

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