Literature DB >> 204352

On the mechanism of the acceleration of methanesulfonylation of acetylcholinesterase with cationic accelerators.

M R Pavlic, I B Wilson.   

Abstract

1. In order to elucidate some features of the mechanism of the acceleration of methanesulfonylation of acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) with cationic accelerators, the methanesulfonylation of this enzyme by high concentrations of methanesulfonylfluoride, in the absence and presence of accelerators decamethonium and tetraethylammonium, was studied. 2. The results showed that the accelerator accelerates the reaction by electrostatically improving the binding between acetylcholinesterase and methanesulfonylfluoride without effecting the rate of the decomposition of the enzyme-inhibitor complex into the methanesulfonylated enzyme and product.

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Year:  1978        PMID: 204352     DOI: 10.1016/0005-2744(78)90013-x

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  4 in total

Review 1.  Utilization of the free energy of the reversible binding of protein and modifying agent towards the rate-enhancement of protein covalent modification.

Authors:  E T Rakitzis
Journal:  Biochem J       Date:  1990-08-01       Impact factor: 3.857

2.  Potentiation effect of choline esters on choline-catalysed decarbamoylation of dimethylcarbamoyl-acetylcholinesterase.

Authors:  Y B Kim; C H Jung; S J Choi; W J Seo; S H Cha; D E Sok
Journal:  Biochem J       Date:  1992-05-15       Impact factor: 3.857

Review 3.  Kinetics of protein modification reactions.

Authors:  E T Rakitzis
Journal:  Biochem J       Date:  1984-01-15       Impact factor: 3.857

4.  Multiple binding sites involved in the effect of choline esters on decarbamoylation of monomethylcarbamoyl- or dimethylcarbamoly-acetylcholinesterase.

Authors:  D E Sok; Y B Kim; S J Choi; C H Jung; S H Cha
Journal:  Biochem J       Date:  1994-08-01       Impact factor: 3.857

  4 in total

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