Why acetylcholinesterase reactivators do not work in butyrylcholinesterase

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Authors

WIESNER Jiří KŘÍŽ Zdeněk KUČA Kamil JUN Daniel KOČA Jaroslav

Year of publication 2010
Type Article in Periodical
Magazine / Source Journal of Enzyme Inhibition and Medicinal Chemistry
MU Faculty or unit

Faculty of Science

Citation
Field Physical chemistry and theoretical chemistry
Keywords butyrylcholinesterase; acetylcholinesterase; reactivation; pyridinium oximes; reactivator aromatic binding pocket; peripheral anionic site
Description 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 blood with the simultaneous administration of butyrylcholinesterase reactivators, when the enzyme is continuously reactivated by oxime. This article summarises and sets forth the structural differences between butyrylcholinesterase and acetylcholinesterase essential for 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, while used in butyrylcholinesterase, non-functional.
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