Contribution of Aromatic Moieties of Tyrosine 133 and of the Anionic Subsite Tryptophan 86 to Catalytic Efficiency and Allosteric Modulation of Acetylcholinesterase-Reference-Cited by-同舟云学术

Contribution of Aromatic Moieties of Tyrosine 133 and of the Anionic Subsite Tryptophan 86 to Catalytic Efficiency and Allosteric Modulation of Acetylcholinesterase

Published:1995-02 Issue:5 Volume:270 Page:2082-2091
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Ordentlich Arie,Barak Dov,Kronman Chanoch,Ariel Naomi,Segall Yoffi,Velan Baruch,Shafferman Avigdor

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference54 articles.

1. Structure and dynamics of the active site gorge of acetylcholinesterase: Synergistic use of molecular dynamics simulation and X-ray crystallography

2. Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common core.

3. Catalysis by acetylcholinesterase. Acceleration of the hydrolysis of neutral acetic acid esters by certain aromatic cations.

4. Kinetic, equilibrium and spectroscopic studies on cation association at the active center of acetylcholinesterase: topographic distinction between trimethyl and trimethylammonium sites

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