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Acetylchloinesterase (AChE) is an enzyme that catalyzes the conversion of acetylcholine to choline and acetic acid thus inactivating the neurotransmitter.

AChE is found in cholinergic neurons, and is highly concentrated at the postsynaptic end plate of the neuromuscular junction. It is one of the most efficient enzymes known: one molecule of AChE can hydrolyze 6 x 105 ACh molecules per minute; this yields a turnover time of 150 microseconds.

AChE also has been proposed to have multiple nonclassical biological functions which include neuritogenesis, cell adhesion, synaptogenesis, amyloid fiber assembly, activation of dopamine receptors, hematopoiesis, and thrombopoiesis. These functions remain controversial.

Finally, AChE inhibitors have important pharmacologic effects.


  1. Goodman LS, Gilman A, Brunton LL, Lazo JS, Parker KL. Goodman & Gilman's the pharmacological basis of therapeutics. 11th / ed. New York: McGraw-Hill; 2006.
  2. Soreq H, Seidman S. Acetylcholinesterase--new roles for an old actor. Nat Rev Neurosci 2001;2(4):294-302.
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