Conference paper

Structural Changes in Acetylcholinesterase under the Influence of Some Ligands

Miloš R. Pavlič ; Institute of Biochemistry and Institute of Pathophysiology, Medical Faculty, University of Ljubljana, 61000 Ljubljana, Yugoslavia

Abstract

In order to elucidate the nature of the effect of some ligands
on the methanesulfonylation of acetylcholinesterase (acetylcholine
acetylhydrolase, EC 3.1.1.7), the methanesulfonylation of the enzyme
was studied, in the absence and presence of ligands, at various
temperatures and at various dielectric consfants. The thermodynamic
quantities obtained for the overall reaction, Li H=I=, Li S=I=,
and Li G=I=, point to specific structural chacri.ges in the esteratic
site of the enzyme under the influence of accelerators of methanesulfonylation but do not clearly answer the question about the
nature of the effect of the ligands. A closer analysis of the
activation entropy for the reaction in the absence and presence
of decamethonium indicates that the acceleration effect of this
ligand on the methanesulfonylation of acetylcholinesterase is an
electrostatic effect and is associated with a relatively less favourable
conformational change in the esteratic site of the enzyme.

Keywords

Hrčak ID:

196613

URI

https://hrcak.srce.hr/196613

Publication date:

3.12.1975.

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