Acetyl cholinesterase: Difference between revisions
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Acetyl cholinesterase (AChE) is an enzyme with a catalytic function of hydrolysing the [[Neurotransmitter|neurotransmitter]] [[Acetylcholine|acetylcholine (Ach)]] into its two elements: choline and acetate. This reaction happens at the junctional fold in the [[ | Acetyl cholinesterase (AChE) is an enzyme with a catalytic function of hydrolysing the [[Neurotransmitter|neurotransmitter]] [[Acetylcholine|acetylcholine (Ach)]] into its two elements: choline and acetate. This reaction happens at the junctional fold in the [[Synaptic cleft|synaptic cleft]] where acetylcholine is exported out by the [[Secretory_vesicles|secretory vesicles]] from the [[Presynaptic knob|presynaptic knob]] and flow across the synapse. The acetylcholine interact and bind to the [[Postsynaptic receptor|postsynaptic receptor]] to transmit the signal.<ref>Daniel MQ. Acetylcholinesterase : Enzyme Structure, Reaction Dynamics, and Virtual Transition States. Chem. Rev., 1987, 87 (5), pp 955–979. This is available from DOI: 10.1021/cr00081a005.</ref> The removal of neurotransmitter after the [[Signal transmission|signal transmission]] at the [[Postsynaptic membrane|postsynaptic membrane]] is vital in order to enable the generation of new [[Action potential|action potential]] by [[Stimulus|stimulus]]. | ||
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Revision as of 02:11, 23 November 2018
Acetyl cholinesterase (AChE) is an enzyme with a catalytic function of hydrolysing the neurotransmitter acetylcholine (Ach) into its two elements: choline and acetate. This reaction happens at the junctional fold in the synaptic cleft where acetylcholine is exported out by the secretory vesicles from the presynaptic knob and flow across the synapse. The acetylcholine interact and bind to the postsynaptic receptor to transmit the signal.[1] The removal of neurotransmitter after the signal transmission at the postsynaptic membrane is vital in order to enable the generation of new action potential by stimulus.
Reference
- ↑ Daniel MQ. Acetylcholinesterase : Enzyme Structure, Reaction Dynamics, and Virtual Transition States. Chem. Rev., 1987, 87 (5), pp 955–979. This is available from DOI: 10.1021/cr00081a005.