Interaction between the peripheral site residues of human butyrylcholinesterase, D70 and Y332, in binding and hydrolysis of substrates (Q78122923)

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11 December 2019

title

Interaction between the peripheral site residues of human butyrylcholinesterase, D70 and Y332, in binding and hydrolysis of substrates (English)

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11 December 2019

1

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11 December 2019

author name string

W Xie

2

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11 December 2019

M T Froment

3

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11 December 2019

V Levitsky

4

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P L Fortier

5

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C Albaret

6

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O Lockridge

7

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11 December 2019

language of work or name

English

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publication date

1 August 1999

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11 December 2019

number of pages

13

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Biochimica et Biophysica Acta

inferred from page(s)

published in

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volume

1433

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11 December 2019

issue

1-2

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page(s)

281-293

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Molecular and cellular biology of cholinesterases

11 December 2019

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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors

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Asp7O in the peripheral anionic site of human butyrylcholinesterase

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Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase

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Trp82 and Tyr332 are involved in two quaternary ammonium binding domains of human butyrylcholinesterase as revealed by photoaffinity labeling with [3H]DDF.

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Horse serum butyrylcholinesterase kinetics: a molecular mechanism based on inhibition studies with dansylaminoethyltrimethylammonium

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Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect

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Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite.

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Differences in active site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase

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Polyol-induced activation by excess substrate of the D70G butyrylcholinesterase mutant

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Sulphur and selenium compounds related to acetylcholine and choline—VIII. Comparative studies of succinoylcholine, succinoylthiolcholine and succinoylselenolcholine

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A new and rapid colorimetric determination of acetylcholinesterase activity

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Identifiers

DOI

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11 December 2019

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