Interactions of Organophosphorus and Carbamate Compounds with Cholinesterases
Toxicology of Organophosphate & Carbamate Compounds, Page: 209-218
2006
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- 19Captures
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Book Chapter Description
Cholinesterases are enzymes that are serine hydrolases that preferentially hydrolyze choline esters. Vertebrates are known to have two cholinesterases, referred to as acetylcholinesterase and butyrylcholinesterase. These two cholinesterases have been differentiated historically on the basis of their substrate selectivity. AChE hydrolyzes acetylcholine (ACh) faster than butyrylcholine (BuCh) or propionylcholine, whereas BuChE metabolizes BuCh and propionylcholine faster than ACh. It is thought that this difference in substrate selectivity to arises from the differences in acyl pocket structure, which, in the case of BuChE, allows access of larger substrates to the active site. AChE is known to play a critical role in the termination of the action of ACh at synapses and neuromuscular junctions, whereas the exact function(s) of BuChE remains unclear. However, numerous potential roles for BuChE have been suggested, ranging from metabolism of lipoproteins to cell adhesion, and the etiology of certain neurodegenerative diseases. Many organophosphorus (OP) and carbamate (CM) compounds exert their acute toxicity through inhibition of AChE. These compounds include all of the OP and most of the CM pesticides, as well as certain chemical warfare agents. Additionally, a limited number of OP and CM drugs exert their therapeutic effects through inhibition of AChE. Inhibition of this critical enzyme leads to an accumulation of ACh at synapses and neuroeffector junctions, which in turn leads to a range of symptoms known as cholinergic crisis.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/B9780120885237500168; http://dx.doi.org/10.1016/b978-012088523-7/50016-8; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=71849104278&origin=inward; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85133597384&origin=inward; https://linkinghub.elsevier.com/retrieve/pii/B9780120885237500168; http://linkinghub.elsevier.com/retrieve/pii/B9780120885237500168; https://dx.doi.org/10.1016/b978-012088523-7/50016-8
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