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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.
Moscow University Chemistry Bulletin.
2018, Vol. 59, No. 4, P. 257
   

Copyright (C) Chemistry Dept., Moscow State University, 2002
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