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Anastasia R. Blinova, Anna M. Kulakova, Bella L. Grigorenko
Mechanism of
deprotonation of the amino group of glutamate upon binding to N-acetylglutamate
synthase
Abstract
Abstract. Gcn5-related
N-acetyltransferases catalyze the transfer of an acetyl group to a primary
amino group of a wide class of substrates. Protonation of the amino group upon
binding to the enzyme is necessary to activate the nucleophilic attack on the
substrate. The process of glutamate binding to N-acetylglutamate synthase is
considered using molecular modeling and quantum chemistry methods. It has been
shown that deprotonation of the primary amino group of glutamate occurs upon
binding to the active site of the enzyme with the participation of the side
chain of the aspartate residue.
Key words:
acetyltransferases, protonation state, molecular dynamics, QM/MM, Gibbs energy.
Copyright (C) Chemistry Dept., Moscow State University, 2002
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