Base-catalyzed and cholinesterase-catalyzed hydrolysis of acetylcholine and optically active analogs

The base- and cholinestrase-catalyzed hydrolyses of the following optically active analogs of acetylcholine were studied: 3 (a)-trimethylammonium-2(a)-acetoxy-trans-decalin iodide, threo- and erythro-alpha, beta-dimethylacetylcholine iodide, alpha-methylacetylcholine, and beta-methylacetylcholine. E...

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Bibliographic Details
Published in:Journal of medicinal chemistry 1975-03, Vol.18 (3), p.292-300
Main Authors: Schowen, Katharine B, Smissman, Edward E, Stephen, William F
Format: Article
Language:English
Subjects:
Acetylcholine - analogs & derivatives
Animals
Binding Sites
Catalysis
Cattle
Chemical Phenomena
Chemistry
Cholinesterases
Electrophorus
Erythrocytes - enzymology
Hydrolysis
Kinetics
Molecular Conformation
Optical Rotation
Quantum Theory
Stereoisomerism
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Summary:The base- and cholinestrase-catalyzed hydrolyses of the following optically active analogs of acetylcholine were studied: 3 (a)-trimethylammonium-2(a)-acetoxy-trans-decalin iodide, threo- and erythro-alpha, beta-dimethylacetylcholine iodide, alpha-methylacetylcholine, and beta-methylacetylcholine. Evidence that the optimum dihedral +N-C-C-O angle in the transition state for acetylcholinesterase hydrolysis of acetylcholine analogs is positive and anticlinal is given. The data obtained suggest that acetylcholine undergoes a geometrically flexible mode of attachment to the enzyme.
ISSN:0022-2623
1520-4804
DOI:10.1021/jm00237a017