The Mechanism of Deprotonation of the Amino Group of Glutamate upon Binding to N-Acetylglutamate Synthase

Abstract

Gcn5-related N-acetyltransferases catalyze the transfer of an acetyl group to a primary amino group of a wide class of substrates. Deprotonation of the amino group upon binding to the enzyme is necessary to activate the nucleophilic attack on the substrate. The process of binding of glutamate to N-acetylglutamate synthase is considered using the methods of molecular modeling and quantum chemistry. It is shown that deprotonation of the primary amino group of glutamate occurs upon its incorporation into the active site of the enzyme with the participation of the side chain of the aspartate residue.