Effect of electrostatic interactions in recognition of acetylcholine by acetylcholinesterase

Document Type

Article

Publication Date

2-19-1998

Abstract

The role of electrostatic interactions in the steering of acetylcholine to the active site of acetylcholinesterase is investigated in this study. The results obtained suggest that acetylcholinesterase's catalytic processes involve more than two steps, one of which appears to be diffusion-controlled, while the others are influenced by electrostatic interactions. The results also support the concept that the electrostatic field contributes to the guidance of the ligand upon its close proximity to the entrance of the active site gorge. On the basis of the data obtained, a prehydrolysis (pre-transition state) structure for this catalytic reaction is also proposed. The root mean square deviation of the Ca atoms of the amino acid residues of the active site between the proposed transition state and a recently proposed transition state based on experimental data is 0.379 Å. © 1998 Elsevier Science B.V.

Identifier

0042858534 (Scopus)

Publication Title

Journal of Molecular Structure THEOCHEM

External Full Text Location

https://doi.org/10.1016/S0166-1280(97)00128-0

ISSN

01661280

First Page

81

Last Page

85

Issue

1-2

Volume

425

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