Cholinesterase (ChE) (ChE)

Cholinesterases are a group of serine hydrolases that catalyze the hydrolysis of the neurotransmitter acetylcholine into choline and acetic acid, thereby terminating its action at the synapse [6, 22]. There are two primary types: acetylcholinesterase (AChE), which is found in the nervous system, neuromuscular junctions, and red blood cells, and butyrylcholinesterase (BChE), also known as pseudocholinesterase, which is primarily synthesized in the liver and found in the blood plasma [7, 15]. These enzymes are critical for the proper functioning of the central and peripheral nervous systems, as they prevent the overaccumulation of acetylcholine and subsequent overstimulation of cholinergic receptors [11, 15]. In therapeutic contexts, cholinesterase inhibitors are used to treat neurodegenerative diseases like Alzheimer's disease and neuromuscular disorders such as myasthenia gravis [1, 13]. They also serve as targets for toxic agents, including organophosphate pesticides and nerve gases, which cause a cholinergic crisis by irreversibly inhibiting the enzymes [9, 22]. Furthermore, serum cholinesterase levels are used as biomarkers for liver function and pesticide exposure, while genetic deficiencies in BChE can lead to prolonged paralysis after the administration of certain muscle relaxants [14, 15, 20].

Other names

AcetylcholinesteraseButyrylcholinesterasePseudocholinesteraseTrue cholinesterasePlasma cholinesteraseErythrocyte cholinesteraseAChEBChESChEPChEAcetylcholine acetylhydrolaseAcylcholine acylhydrolase

Reversible or irreversible inhibition of the enzyme to increase synaptic acetylcholine levels; Reactivation of the enzyme using oximes to restore activity after organophosphate poisoning [9, 11, 13, 22].