Abstract
The two classes of human cholinesterases (CHEs), acetylcholinesterase(acetylcholine acetyl hydrolase, ACHE, EC 3.1.1.7) and butyrylcholinesterase (acylcholine acyl hydrolase, BCHE, EC 3.1.1.8) are highly homologous proteins capable of rapidly hydrolyzing choline estersl. Despite their similar mechanisms of action, they differ in substrate specificity and sensitivity to various inhibitors1,2. Recent advances including cloning,3–6 expression,5,7–10 and 3 dimensional structural analysis of members of the CHE superfamily,11,12 now enable the dissection of functional domains thereof. Within these domains, key amino acids are found which may be implicated in catalysis or in binding of various ligands. The disclosing of such key residues could lead to designing of novel therapeutic agents as well as to the unravelling of the molecular mechanisms underlying the functioning of ChEs.
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Gnatt, A., Loewenstein, Y., Soreq, H. (1992). Molecular Dissection of Functional Domains in Human Cholinesterases Expressed in Microinjected Xenopus Oocytes. In: Shafferman, A., Velan, B. (eds) Multidisciplinary Approaches to Cholinesterase Functions. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3046-6_21
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DOI: https://doi.org/10.1007/978-1-4615-3046-6_21
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