Fasciculin 2 Binds to the Peripheral Site on Acetylcholinesterase and Inhibits Substrate Hydrolysis by Slowing a Step Involving Proton Transfer during Enzyme Acylation
Open Access
- 1 August 1995
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 270 (34) , 19694-19701
- https://doi.org/10.1074/jbc.270.34.19694
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Study of structure-activity relationship of fasciculin by acetylation of amino groupsBiochimica et Biophysica Acta (BBA) - General Subjects, 1994
- Nitrogen isotope effects on acetylcholinesterase-catalyzed hydrolysis of o-nitroacetanilideJournal of the American Chemical Society, 1993
- Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitorsBiochemistry, 1993
- An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase.Proceedings of the National Academy of Sciences, 1993
- 1.9-A resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba snake venom.Journal of Biological Chemistry, 1992
- Ligand exclusion on acetylcholinesteraseBiochemistry, 1990
- Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition statesChemical Reviews, 1987
- Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligandsBiochemistry, 1980
- A new and rapid colorimetric determination of acetylcholinesterase activityBiochemical Pharmacology, 1961
- Molecular Mechanisms for Hydrolytic Enzyme Action. III. A General Mechanism for the Inhibition of AcetylcholinesteraseJournal of the American Chemical Society, 1961