Role of ionic interactions in cholinesterase catalysis
- 1 November 1996
- journal article
- review article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1298 (1), 12-30
- https://doi.org/10.1016/s0167-4838(96)00128-8
Abstract
No abstract availableKeywords
This publication has 105 references indexed in Scilit:
- pH-dependent salting-out effect in enzyme-catalyzed reaction kineticsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- Kinetic, equilibrium and spectroscopic studies on cation association at the active center of acetylcholinesterase: topographic distinction between trimethyl and trimethylammonium sitesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Tailoring the pH dependence of enzyme catalysis using protein engineeringNature, 1985
- 412 — Polyelectrolyte field effectsBioelectrochemistry and Bioenergetics, 1981
- Ion effects on ligand-nucleic acid interactionsJournal of Molecular Biology, 1976
- Inorganic ion effects on the kinetic parameters of acetylcholinesteraseJournal of Neurochemistry, 1973
- On the specificity of tryptic catalysisBiochemical and Biophysical Research Communications, 1971
- A Simple Model of Molecular Specificity in Enzyme-Substrate Systems. I. Theory and Applications to the System Acetylcholinesterase-SubstrateJournal of the American Chemical Society, 1955
- Fine structure of the active surface of cholinesterases and the mechanism of enzymatic ester hydrolysisDiscussions of the Faraday Society, 1955
- The structure of the active surface of serum cholinesteraseBiochimica et Biophysica Acta, 1954