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Pomacea canaliculata acetylcholinesterase (PcAChE) is a critical enzyme in the nervous system of the golden apple snail, where it regulates the levels of the neurotransmitter acetylcholine [1]. Its primary biological function is the rapid hydrolysis of acetylcholine at the synaptic cleft, which is essential for terminating nerve impulses and maintaining normal neuromuscular function [2]. As the golden apple snail is a destructive invasive species and a vector for the human parasite Angiostrongylus cantonensis, PcAChE is a major target for chemical control strategies [3]. Various molluscicides, including organophosphates like chlorpyrifos and carbamates like carbaryl, act by inhibiting this enzyme, leading to an overaccumulation of acetylcholine [4]. This inhibition results in continuous nerve firing, leading to paralysis and death of the snail [5]. However, the use of these inhibitors poses significant safety challenges due to their lack of specificity, often resulting in toxicity to non-target aquatic organisms and potential neurotoxic risks to humans [6]. Consequently, research is ongoing to develop more selective PcAChE inhibitors that can effectively manage snail populations while minimizing environmental and health impacts [7].
Inhibition of acetylcholine hydrolysis through covalent or non-covalent binding to the enzyme active site, leading to neuromuscular overstimulation and paralysis.
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