On the mechanism of the acceleration of methanesulfonylation of acetylcholinesterase with cationic accelerators
- PMID: 204352
- DOI: 10.1016/0005-2744(78)90013-x
On the mechanism of the acceleration of methanesulfonylation of acetylcholinesterase with cationic accelerators
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.
Similar articles
-
The acceleration of methanesulfonylation of acetylcholinesterase with cationic accelerators as an electrostatic effect.Biochim Biophys Acta. 1978 Jun 9;524(2):340-8. doi: 10.1016/0005-2744(78)90170-5. Biochim Biophys Acta. 1978. PMID: 208619
-
On the nature of the acceleration of the methanesulfonylation of acetylcholinesterase by tetraethylammonium.Biochim Biophys Acta. 1973 Dec 19;327(2):393-7. doi: 10.1016/0005-2744(73)90422-1. Biochim Biophys Acta. 1973. PMID: 4360429 No abstract available.
-
The role of hydration in an enzyme reaction.Arch Biochem Biophys. 1987 Mar;253(2):446-52. doi: 10.1016/0003-9861(87)90198-6. Arch Biochem Biophys. 1987. PMID: 3566286
-
Acceleration of Drosophila melanogaster acetylcholinesterase methanesulfonylation: peripheral ligand D-tubocurarine enhances the affinity for small methanesulfonylfluoride.Chem Biol Interact. 2002 Feb 20;139(2):145-57. doi: 10.1016/s0009-2797(01)00294-0. Chem Biol Interact. 2002. PMID: 11823003
-
Computational Studies on Acetylcholinesterases.Molecules. 2017 Aug 10;22(8):1324. doi: 10.3390/molecules22081324. Molecules. 2017. PMID: 28796192 Free PMC article. Review.
Cited by
-
Kinetics of protein modification reactions.Biochem J. 1984 Jan 15;217(2):341-51. doi: 10.1042/bj2170341. Biochem J. 1984. PMID: 6365085 Free PMC article. Review. No abstract available.
-
Utilization of the free energy of the reversible binding of protein and modifying agent towards the rate-enhancement of protein covalent modification.Biochem J. 1990 Aug 1;269(3):835-8. doi: 10.1042/bj2690835. Biochem J. 1990. PMID: 2202295 Free PMC article. Review.
-
Multiple binding sites involved in the effect of choline esters on decarbamoylation of monomethylcarbamoyl- or dimethylcarbamoly-acetylcholinesterase.Biochem J. 1994 Aug 1;301 ( Pt 3)(Pt 3):713-20. doi: 10.1042/bj3010713. Biochem J. 1994. PMID: 8053896 Free PMC article.
-
Potentiation effect of choline esters on choline-catalysed decarbamoylation of dimethylcarbamoyl-acetylcholinesterase.Biochem J. 1992 May 15;284 ( Pt 1)(Pt 1):153-60. doi: 10.1042/bj2840153. Biochem J. 1992. PMID: 1599395 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials