Acetylcholinesterase (Electrophorus electricus) (AChE)

Acetylcholinesterase (AChE) from the electric eel (Electrophorus electricus) is a serine hydrolase that plays a vital role in the cholinergic nervous system by rapidly terminating synaptic transmission through the hydrolysis of acetylcholine (UniProt P00738). It is particularly abundant in the electric organ of the eel, making it one of the most extensively studied enzymes in biochemistry and pharmacology (PubMed: 1564350). While the eel enzyme itself is not a human therapeutic target, it serves as a gold-standard surrogate and model system for human AChE in drug discovery and toxicology (PubMed: 25863512). Researchers utilize eel AChE to screen for potential treatments for Alzheimer's disease, as well as to study the effects of nerve agents and pesticides (PubChem AID 1194). Drugs that interact with this enzyme, such as donepezil and galantamine, function by reversibly or irreversibly binding to its active site, thereby enhancing cholinergic signaling (StatPearls: Cholinesterase Inhibitors).

Other names

True cholinesteraseAcetylcholine acetylhydrolaseEeAChEElectric eel acetylcholinesterase

Inhibition of the enzyme's catalytic activity, leading to increased levels and duration of action of the neurotransmitter acetylcholine at the synaptic cleft (StatPearls: Cholinesterase Inhibitors).