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. 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.
D000109:Acetylcholine / Q000031:analogs & derivatives*; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002802:Cholinesterases; D004593:Electrophorus; D004912:Erythrocytes / Q000201:enzymology; D006868:Hydrolysis; D007700:Kinetics; D008968:Molecular Conformation; D009904:Optical Rotation; D011789:Quantum Theory; D013237:Stereoisomerism
D002802:Cholinesterases; D000109:Acetylcholine