Why acetylcholinesterase reactivators do not work in butyrylcholinesterase
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Acetylcholinesterase chemistry MeSH
- Antidotes chemistry MeSH
- Butyrylcholinesterase chemistry MeSH
- Protein Conformation MeSH
- Humans MeSH
- Models, Molecular MeSH
- Mice MeSH
- Organophosphate Poisoning MeSH
- Oximes chemistry therapeutic use MeSH
- Cholinesterase Reactivators chemistry MeSH
- Binding Sites MeSH
- Structure-Activity Relationship MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Acetylcholinesterase MeSH
- Antidotes MeSH
- Butyrylcholinesterase MeSH
- Oximes MeSH
- Cholinesterase Reactivators MeSH
The pyridinium oxime therapy for treatment of organophosphate poisoning is a well established, but not sufficient method. Recent trends also focus on prophylaxis as a way of preventing even the entrance of organophosphates into the nervous system. One of the possible prophylactic methods is increasing the concentration of butyrylcholinesterase in the blood with the simultaneous administration of butyrylcholinesterase reactivators, when the enzyme is continuously reactivated by oxime. This article summarizes and sets forth the structural differences between butyrylcholinesterase and acetylcholinesterase, essential for the future design of butyrylcholinesterase reactivators. Butyrylcholinesterase lacks the reactivator aromatic binding pocket found in acetylcholinesterase, which is itself a part of the acetylcholinesterase peripheral anionic site. This difference finally renders the current acetylcholinesterase reactivators, when used in butyrylcholinesterase, non-functional.
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