Stereospecificity of hydrolytic enzymes in their reaction with optically active organophosphorus compounds; I. The reaction of cholinesterases and paraoxonase with S-alkyl p-nitrophenyl methylphosphonothiolates
article
Reaction velocities of the irreversible inhibition of acetylcholinesterase and butyrylcholinesterase by a series of optically active S-alkyl p-nitrophenyl methylphosphonothiolates have been determined, as well as the rates of hydrolysis of these phosphorus compounds by sheep serum paraoxonase. Acetylcholinesterase proved to be much more stereospecific than butyrylcholinesterase. A rough correlation between the stereospecificity of acetylcholinesterase and inhibitor activity exists. Sheep serum paraoxonase likewise shows a definite stereospecificity for this particular series of compounds. It hydrolyses preferentially the enantiomeric series with the lowest anticholinesterase activity. © 1965.
Chemicals/CAS: acetylcholinesterase, 9000-81-1; cholinesterase, 9001-08-5; phosphatase, 9013-05-2; Acetylcholinesterase, EC 3.1.1.7; Cholinesterase Inhibitors; Cholinesterases, EC 3.1.1.8; Enzymes; Phosphonic Acids; Phosphoric Monoester Hydrolases, EC 3.1.3
Chemicals/CAS: acetylcholinesterase, 9000-81-1; cholinesterase, 9001-08-5; phosphatase, 9013-05-2; Acetylcholinesterase, EC 3.1.1.7; Cholinesterase Inhibitors; Cholinesterases, EC 3.1.1.8; Enzymes; Phosphonic Acids; Phosphoric Monoester Hydrolases, EC 3.1.3
Topics
TNO Identifier
356970
Source
Biochemical pharmacology, 14(12), pp. 1839-1845.
Pages
1839-1845
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