TAILIEUCHUNG - Báo cáo khoa học: Kinetics of inhibition of acetylcholinesterase in the presence of acetonitrile

The hydrolysis of acetylthiocholine by acetylcholinesterase fromElectro-phorus electricuswas investigated in the presence of the inhibitors tacrine, gallamine and compound1. The interaction of the enzyme with the sub-strate and the inhibitors was characterized by the parametersKI , a¢, borb, Kmand Vmax, which were determined directly and simultaneously from nonlinear Michaelis–Menten plots. | ễFEBS Journal Kinetics of inhibition of acetylcholinesterase in the presence of acetonitrile Markus Pietsch Leonie Christian Therese Inhester Susanne Petzold and Michael Gutschow PharmaceuticalChemistry I Pharmaceutical institute University of Bonn Germany Keywords acetylcholinesterase enzyme kinetics gallamine triethiodide hyperbolic mixed-type inhibition tacrine hydrochloride Correspondence M. Pietsch Schoolof Chemistry Physics The University of Adelaide Adelaide SA 5005 Australia Fax 61 8 8303 4358 Tel 61 8 8303 5360 E-mail Received 15 August 2008 revised 10 January 2009 accepted 11 February 2009 doi The hydrolysis of acetylthiocholine by acetylcholinesterase from Electrophorus electricus was investigated in the presence of the inhibitors tacrine gallamine and compound 1. The interaction of the enzyme with the substrate and the inhibitors was characterized by the parameters KI a b or b Km and Vmax which were determined directly and simultaneously from nonlinear Michaelis-Menten plots. Tacrine was shown to act as a mixed-type inhibitor with a strong noncompetitive component a w 1 and to completely block deacylation of the acyl-enzyme. In contrast acetylcholinesterase inhibition by gallamine followed the steric blockade hypothesis . only substrate association to as well as substrate product dissociation from the active site were reduced in the presence of the inhibitor. The relative efficiency of the acetylcholinesterase-gallamine complex for the catalysis of substrate conversion was determined to be of that of the free enzyme. Substrate hydrolysis and the inhibition of acetylcholinesterase were also investigated in the presence of 6 acetonitrile and a competitive pseudo-inhibition was observed for acetonitrile KI M . The interaction of acetylcholinesterase with acetonitrile and tacrine or gallamine resulted in a seven- to 10-fold increase in the KI values whereas the principal mode of

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