BChE

Butyrylcholinesterase (BChE, EC 3.1.1.8) is a cholinesterase family enzyme that hydrolyzes a broad range of choline esters and other ester-containing substrates, contributing to cholinergic regulation as well as xenobiotic detoxification processes^[1][2]. BChE is widely distributed in human tissues and plasma, where it participates in cholinergic transmission, ester metabolism, and the neutralization of toxic compounds including organophosphates and carbamates^[1]. Mechanistically, BChE functions as a hydrolytic enzyme that can buffer acetylcholine metabolism when acetylcholinesterase (AChE) activity is reduced, thereby influencing cholinergic homeostasis^[2]. In disease contexts, increasing evidence links BChE to neurodegenerative disorders, particularly Alzheimer’s disease (AD), where BChE activity and expression become more prominent during disease progression and are associated with late-stage cholinergic dysfunction^[3][4]. Experimental studies therefore consider BChE an important therapeutic target and biomarker candidate for AD-related research^[3][4]. Compared with the closely related isoform AChE, which primarily terminates synaptic acetylcholine signaling, BChE exhibits broader substrate specificity, distinct tissue distribution, and a stronger role in drug metabolism, detoxification, and non-neuronal physiological processes^[1][2]. For experimental applications, selective BChE inhibitors are widely used to investigate cholinergic mechanisms and have been developed as pharmacological tools for evaluating therapeutic strategies in neurodegenerative disease models, with high selectivity over AChE considered a key design objective^[3][4].