Mechanism of enzymic hydrolysis I. Role of the acidic group in the estetratic site of acetylcholinesterase

作者: Irwin B. Wilson

DOI: 10.1016/0006-3002(51)90050-9

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摘要: Measurements of the inhibition acetylcholinesterase by prostigmine as a function pH under non-competitive conditions reveal that basic group in esteratic site enzyme is essential for formation substrate complex but tha] acid not significantly involved. The hydrolytic process which follows enzyme-substrate complex. These conclusions are accordance with previously developed mechanism catalyzed hydrolysis. The measured dissociation constant and free enzyme.

参考文章(6)
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Felix. Bergmann, Irwin B. Wilson, David. Nachmansohn, Acetylcholinesterase. IX. Structural features determining the inhibition by amino acids and related compounds. Journal of Biological Chemistry. ,vol. 186, pp. 693- 703 ,(1950) , 10.1016/S0021-9258(18)56262-1
Klas-Bertil Augustinsson, David Nachmansohn, STUDIES ON CHOLINESTERASE VI. KINETICS OF THE INHIBITION OF ACETYLCHOLINE ESTERASE Journal of Biological Chemistry. ,vol. 179, pp. 543- 559 ,(1949) , 10.1016/S0021-9258(19)51250-9
Irwin B. Wilson, Felix. Bergmann, David. Nachmansohn, ACETYLCHOLINESTERASE X. MECHANISM OF THE CATALYSIS OF ACYLATION REACTIONS Journal of Biological Chemistry. ,vol. 186, pp. 781- 790 ,(1950) , 10.1016/S0021-9258(18)56271-2
Irwin B. Wilson, Felix. Bergmann, Acetylcholinesterase. VIII. Dissociation constants of the active groups. Journal of Biological Chemistry. ,vol. 186, pp. 683- 692 ,(1950) , 10.1016/S0021-9258(18)56261-X