Butyrylcholinesterase (BuChE) (BuChE)

Butyrylcholinesterase (BuChE), also known as pseudocholinesterase, is a serine hydrolase enzyme primarily synthesized in the liver and secreted into the plasma [1, 9]. While it shares structural similarities with acetylcholinesterase (AChE), BuChE possesses a broader substrate specificity, allowing it to hydrolyze various choline esters, including acetylcholine and butyrylcholine, as well as exogenous toxins and drugs like cocaine and succinylcholine [6, 14]. In the healthy brain, AChE is the primary regulator of cholinergic signaling; however, in Alzheimer's disease, BuChE activity progressively increases while AChE levels decline, making BuChE a critical therapeutic target for maintaining acetylcholine levels and potentially slowing neurodegeneration [3, 8]. Beyond its role in the nervous system, BuChE acts as a natural bioscavenger against organophosphate nerve agents and pesticides by neutralizing them before they reach their primary targets [14, 16]. Genetic variants of the BCHE gene can lead to deficiency, resulting in life-threatening prolonged apnea when patients are administered certain neuromuscular blocking agents during surgery [1, 18]. Recent research also highlights its role in metabolic regulation through the hydrolysis of the hunger hormone ghrelin, suggesting potential applications in treating obesity and metabolic syndrome [11, 16].

Other names

PseudocholinesterasePlasma cholinesteraseBCHECholinesterase (non-specific)Acylcholine acylhydrolaseCholine esterase IIBenzoylcholinesterase

Reversible or irreversible inhibition of the enzyme's catalytic activity to increase synaptic acetylcholine levels or prevent the metabolism of specific substrates; stoichiometric bioscavenging of organophosphate toxins.