Acetylcholinesterase

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Acetylcholinesterase (pronunciation: a-se-til-ko-li-nes-ter-ase, /əˌsɛtɪlkəʊlɪˈnɛstəreɪz/) is an important enzyme that primarily functions in the termination of synaptic transmission by rapidly hydrolyzing the neurotransmitter Acetylcholine. It is found at mainly at neuromuscular junctions and cholinergic brain synapses, where its activity serves to terminate synaptic transmission.

Etymology

The term "Acetylcholinesterase" is derived from its role in the breakdown of the neurotransmitter acetylcholine. "Acetyl" refers to the acetyl group (CH3CO), "choline" is a quaternary ammonium salt, and "esterase" is a type of enzyme that breaks down esters.

Function

Acetylcholinesterase's primary function is to break down Acetylcholine in the synaptic cleft immediately following its release from the presynaptic neuron. This rapid removal of acetylcholine prevents continuous activation of the postsynaptic cell and allows for precise control of the duration and intensity of synaptic signals.

Related Terms

  • Neurotransmitter: Chemicals that transmit signals from a neuron to a target cell across a synapse.
  • Synapse: A structure that permits a neuron to pass an electrical or chemical signal to another neuron or to the target effector cell.
  • Neuromuscular junction: A chemical synapse formed by the contact between a motor neuron and a muscle fiber.
  • Cholinergic: Referring to cells that use acetylcholine as their synaptic transmitter.

See Also

External links

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