Abstract
The phosphorylation of the serine hydroxyl group in the active site of acetylcholinesterase (AChE) inactivates this essential enzyme in neurotransmission. Oximes are reactivators of AChE phosphorylated by organophosphorus compounds (OP) including insecticides and nerve agents. The effectiveness of oxime-assisted reactivation is primarily attributed to the nucleophilic displacement rate of organophosphate, but efficiency varies with the structure of the bound
Keywords: Acetylcholinesterase, antidote, bioscavenger, butyrylcholinesterase, nerve agents, tabun, oxime, treatment
Current Bioactive Compounds
Title: Cholinesterase Interactions with Oximes
Volume: 6 Issue: 1
Author(s): Z. Kovarik, M. Katalinic, A. Bosak and G. Sinko
Affiliation:
Keywords: Acetylcholinesterase, antidote, bioscavenger, butyrylcholinesterase, nerve agents, tabun, oxime, treatment
Abstract: The phosphorylation of the serine hydroxyl group in the active site of acetylcholinesterase (AChE) inactivates this essential enzyme in neurotransmission. Oximes are reactivators of AChE phosphorylated by organophosphorus compounds (OP) including insecticides and nerve agents. The effectiveness of oxime-assisted reactivation is primarily attributed to the nucleophilic displacement rate of organophosphate, but efficiency varies with the structure of the bound
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Cite this article as:
Kovarik Z., Katalinic M., Bosak A. and Sinko G., Cholinesterase Interactions with Oximes, Current Bioactive Compounds 2010; 6 (1) . https://dx.doi.org/10.2174/157340710790711764
DOI https://dx.doi.org/10.2174/157340710790711764 |
Print ISSN 1573-4072 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-6646 |
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