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Kinetic analysis of butyrylcholinesterase inhibition withN,N-dimethyl-2-phenylaziridinium ion

Authors
Journal
Bioorganic Chemistry
0045-2068
Publisher
Elsevier
Publication Date
Volume
11
Issue
4
Identifiers
DOI: 10.1016/0045-2068(82)90030-x
Disciplines
  • Biology

Abstract

Abstract The kinetics of the butyrylcholinesterase interaction with N,N-dimethyl-2-phenylaziridinium ion, which probably alkylates the anionic site of the enzyme, was investigated at pH 7.5 and 25°C. It was found that the main product of the spontaneous hydrolysis of the aziridinium compound in water, N,N-dimethyl-2-hydroxy-2-phenylethylamine, binds effectively in the enzyme active center and protects it against alkylation. This binding equilibrium as well as the kinetics of the spontaneous decomposition of the aziridinium inhibitor were taken into consideration in calculating the rate and equilibrium constants for the enzyme alkylation reaction. The kinetics of the formation of the aziridinium compound and of the spontaneous hydrolysis reaction were investigated separately at pH 5.8–7.8, and the rate constants obtained from these experiments agree with the corresponding data calculated from the enzyme inhibition kinetics.

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