Human butyrylcholinesterase (BChE)

Human butyrylcholinesterase is a serine hydrolase enzyme broadly distributed in plasma and tissues, structurally related to acetylcholinesterase. It exhibits a wide substrate spectrum, primarily hydrolyzing various esters, including drugs such as succinylcholine, and acting as a natural bioscavenger by binding toxic chemicals (organophosphates, carbamates, cocaine, and related drugs). Modified or engineered variants of human butyrylcholinesterase are developed for enhanced catalytic breakdown of specific toxins, such as nerve agents (e.g., sarin) or drugs of abuse (e.g., cocaine) to serve as potential therapeutics for chemical poisoning or overdose. Its physiological roles extend to cholinergic regulation, inflammation, lipid and ghrelin metabolism, and it functions as a clinical biomarker for liver and systemic health. While exogenous or genetically modified BChE holds promise as an antidote, key challenges include the need for high dosing, immunogenicity concerns, and the specificity and stability of engineered variants[2][3][4][5][6][7].

Other names

Plasma cholinesterasepseudocholinesteraseserum cholinesteraseBCHE proteinCHE2

Hydrolyzes choline esters (breaking down neuromuscular blockers and some drugs) Scavenges and detoxifies organophosphate nerve agents and pesticides by binding and hydrolyzing them Engineered mutants can act as catalytic bioscavengers for faster or expanded detoxification