PMID: 9003439Jan 4, 1997Paper

Kinetic characterization of all steps of the interaction between acetylcholinesterase and eserine

Biochimica Et Biophysica Acta
J Stojan, M Zorko

Abstract

The three-step carbamylenzyme mechanism of the action of eserine on acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) has been known for a long time, but its complete kinetic characterization has never been done. Some of our investigations indicated that the determination of missing kinetic parameters should include the inspection of the enzyme-eserine interaction in a very wide range of eserine concentrations. Therefore, the activity of acetylcholinesterase as a function of time in the presence of low concentrations of eserine comparable to the enzyme concentration was followed. The reaction mechanism was analysed by fitting numerically integrated differential equations that describe the time dependences of all reactants and reaction intermediates to these data. Additionally, the progress curve measurements at higher eserine concentrations were carried out on a stopped-flow apparatus. The corresponding progress curve equations were derived and the kinetic parameters evaluated by non-linear regression treatment. The complex analysis confirmed the three-step mechanism. The values of the constants showed that the very high affinity of eserine for binding into the active centre of the enzyme is not so much a consequ...Continue Reading

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Citations

Mar 26, 2002·Journal of Chemical Information and Computer Sciences·Marko Golicnik
Jan 16, 1999·Journal of Biochemical and Molecular Toxicology·M A Kamal, A A Al-jafari
Jul 25, 1998·The Journal of Biological Chemistry·A OrdentlichA Shafferman
Apr 17, 2012·Natural Product Reports·Malte GerschStephan A Sieber
Sep 13, 2007·Journal of Enzyme Inhibition and Medicinal Chemistry·Ota FekonjaJure Stojan
May 9, 2001·Journal of Enzyme Inhibition·J Stojan

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