Inter-tissue and inter-species comparison of butyrylcholinesterases

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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Inter-tissue and inter-species comparison of butyrylcholinesterases

Abstract: Butyrylcholinesterase (BuChE)

Cited by 2 publications

References 14 publications

Huperzine A from Huperzia serrata: a review of its sources, chemistry, pharmacology and toxicology

Huperzine A from Huperzia serrata: a review of its sources, chemistry, pharmacology and toxicology

Why acetylcholinesterase reactivators do not work in butyrylcholinesterase

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