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E. D. Kots, M. G. Khrenova, S. V. Lushchekina, A. V. Nemukhin
Mechanisms
of regulation of aspartoacylase catalytic activity by results of computer
modeling
Abstract
Results of molecular modeling demonstrate a relation of aspartoacylase
catalytic activity with respect to hydrolysis of N-acetyl-aspartate to
dynamical properties of the dimeric molecule of the enzyme. Availability of the
enzyme active site for the substrate molecule is controlled by conformational
dynamics of peptide chains forming a gate to the transport channel in one of
the monomers. We demonstrate that this model explains the results of
experimental studies showing that the point mutation K213E does not modify
catalytic function of the enzyme.
Key words: enzyme catalysis, aspartoacylase, N-acetyl-aspartate
hydrolysis, protein structure, molecular dynamics, point mutations.
Copyright (C) Chemistry Dept., Moscow State University, 2002
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