Transition State Structure and Rate Determination for the Acylation Stage of Acetylcholinesterase Catalyzed Hydrolysis of (Acetylthio)choline
- 16 March 2000
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 122 (13), 2981-2987
- https://doi.org/10.1021/ja9933590
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Origin of the Catalytic Power of Acetylcholinesterase: Computer Simulation StudiesJournal of the American Chemical Society, 1998
- The X-ray Structure of a Transition State Analog Complex Reveals the Molecular Origins of the Catalytic Power and Substrate Specificity of AcetylcholinesteraseJournal of the American Chemical Society, 1996
- Engineering resistance to ‘aging’ of phosphylated human acetylcholinesterase Role of hydrogen bond network in the active centerFEBS Letters, 1993
- Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitorsBiochemistry, 1993
- Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificityBiochemistry, 1993
- Effect of commitments to catalysis on the degree of curvature in proton inventories of the kinetic parameters for enzyme-catalyzed reactions: application to tryptophan indole-lyaseJournal of the American Chemical Society, 1991
- Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition statesChemical Reviews, 1987
- Fractional diffusion-limited component of reactions catalyzed by acetylcholinesteraseBiochemistry, 1986
- Transition-state structures for ester aminolysis with and without rate-limiting proton transferJournal of the American Chemical Society, 1985
- Kinetics of acetylthiocholine binding to electric eel acetylcholinesterase in glycerol/water solvents of increased viscosity Evidence for a diffusion-controlled reactionBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982