Acetylcholine: Difference between revisions
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<applet load='ACHE2.pdb' size='500' frame='true' align='right' | <applet load='ACHE2.pdb' size='500' frame='true' align='right' | ||
scene='2ace/Ach/ | scene='2ace/Ach/4' /> | ||
[http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase] [http://en.wikipedia.org/wiki/Hydrolysis hydrolysizes] the [http://en.wikipedia.org/wiki/Neurotransmitter neurotransmitter] [http://en.wikipedia.org/wiki/Acetylcholine acetylcholine] <scene name='2ace/Ach/4'>(ACh)</scene>, producing <scene name='2ace/Ach/5'>choline and an acetate</scene> group. <scene name='2ace/Ach/4'>ACh</scene> directly binds <scene name='2ace/Ach/11'>Ser200</scene> (via its [http://en.wikipedia.org/wiki/Nucleophile nucleophilic] Oγ atom) within the [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad] <scene name='2ace/Ach/12'>(Ser200, His440, and Glu327)</scene> ( | [http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase] [http://en.wikipedia.org/wiki/Hydrolysis hydrolysizes] the [http://en.wikipedia.org/wiki/Neurotransmitter neurotransmitter] [http://en.wikipedia.org/wiki/Acetylcholine acetylcholine] <scene name='2ace/Ach/4'>(ACh)</scene>, producing <scene name='2ace/Ach/5'>choline and an acetate</scene> group. <scene name='2ace/Ach/4'>ACh</scene> directly binds <scene name='2ace/Ach/11'>Ser200</scene> (via its [http://en.wikipedia.org/wiki/Nucleophile nucleophilic] Oγ atom) within the [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad] <scene name='2ace/Ach/12'>(Ser200, His440, and Glu327)</scene> of [http://en.wikipedia.org/wiki/Pacific_electric_ray ''Torpedo californica''] [[acetylcholinesterase]] (''Tc''AChE structure [[2ace]]). The residues <scene name='2ace/Ach/13'>Trp84 and Phe330</scene> are also important in the [http://en.wikipedia.org/wiki/Ligand ligand] recognition. | ||
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Revision as of 11:37, 2 March 2010
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Acetylcholine at the Wikipedia
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Acetylcholinesterase hydrolysizes the neurotransmitter acetylcholine , producing group. directly binds (via its nucleophilic Oγ atom) within the catalytic triad of Torpedo californica acetylcholinesterase (TcAChE structure 2ace). The residues are also important in the ligand recognition.