Acetylcholinesterase and Butyrylcholinesterase (AChE and BChE (or BuChE))

Acetylcholinesterase (AChE) is a serine hydrolase enzyme predominantly found at neuromuscular junctions and neural synapses, where it terminates synaptic transmission by rapidly hydrolyzing acetylcholine into choline and acetate[1][3][5]. Butyrylcholinesterase (BChE; historically called pseudocholinesterase) is produced in the liver and located primarily in plasma, responsible for hydrolyzing exogenous esters, including certain anesthetic agents[7]. Both enzymes belong to the carboxylesterase family and are targeted by medically relevant drugs (e.g., AChE inhibitors for Alzheimer's disease) and toxic agents (e.g., nerve gases, organophosphates)[1][2][4][5]. Deficiency of BChE can cause prolonged paralysis after administration of specific muscle relaxants[6]. Both enzymes play critical roles in nervous system function, anesthetic pharmacology, and toxicology.

Other names

AChEacetylcholine acetylhydrolasetrue cholinesterasecholinesterase IacetylhydrolaseBChEBuChEpseudocholinesteraseplasma cholinesterasecholine esterase IIserum cholinesteraseacylcholine acylhydrolase

Inhibition of enzymatic breakdown of acetylcholine, increasing acetylcholine availability at synapses (AChE/BChE inhibitors)\nInhibition by toxicants leading to cholinergic overstimulation, toxicity, or paralysis (e.g., organophosphates, carbamates)\nSubstrate hydrolysis by BChE for drug clearance (succinylcholine, mivacurium)