Neurotransmitters

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'''Under construction!!!'''
'''Under construction!!!'''
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<StructureSection load='' size='400' side='right' scene='82/829381/Cv/1' caption=''>
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<StructureSection load='' size='400' side='right' scene='Acetylcholine/Cv/1' caption=''>
=Acetylcholine=
=Acetylcholine=
[http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase] ([http://www.expasy.org/enzyme/3.1.1.7 EC 3.1.1.7], ''e.g.'' from [http://en.wikipedia.org/wiki/Pacific_electric_ray ''Torpedo californica''], ''Tc''AChE) [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/Cv/2'>(ACh)</scene>, producing <scene name='2ace/Cv/3'>choline and an acetate</scene> group. ACh directly binds <scene name='2ace/Cv/4'>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/Cv/5'>catalytic triad (Ser200, His440, and Glu327)</scene> of (ACh/''Tc''AChE structure [[2ace]]). The residues <scene name='2ace/Cv/6'>Trp84 and Phe330</scene> are also important in the [http://en.wikipedia.org/wiki/Ligand ligand] recognition. After this binding acetylcholinesterase <scene name='2ace/Cv/7'>hydrolysizes</scene> ACh.
[http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase] ([http://www.expasy.org/enzyme/3.1.1.7 EC 3.1.1.7], ''e.g.'' from [http://en.wikipedia.org/wiki/Pacific_electric_ray ''Torpedo californica''], ''Tc''AChE) [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/Cv/2'>(ACh)</scene>, producing <scene name='2ace/Cv/3'>choline and an acetate</scene> group. ACh directly binds <scene name='2ace/Cv/4'>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/Cv/5'>catalytic triad (Ser200, His440, and Glu327)</scene> of (ACh/''Tc''AChE structure [[2ace]]). The residues <scene name='2ace/Cv/6'>Trp84 and Phe330</scene> are also important in the [http://en.wikipedia.org/wiki/Ligand ligand] recognition. After this binding acetylcholinesterase <scene name='2ace/Cv/7'>hydrolysizes</scene> ACh.

Revision as of 16:58, 20 November 2019

Under construction!!!

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References

  1. ↑ Martin JL, Begun J, McLeish MJ, Caine JM, Grunewald GL. Getting the adrenaline going: crystal structure of the adrenaline-synthesizing enzyme PNMT. Structure. 2001 Oct;9(10):977-85. PMID:11591352
  2. ↑ Jones S, Kornblum JL, Kauer JA (August 2000). "Amphetamine blocks long-term synaptic depression in the ventral tegmental area". J. Neurosci. 20 (15): 5575–80. PMID 10908593. http://www.jneurosci.org/cgi/pmidlookup?view=long&pmid=10908593.
  3. ↑ Cruickshank, CC.; Dyer, KR. (Jul 2009). "A review of the clinical pharmacology of methamphetamine.". Addiction 104 (7): 1085–99. doi:10.1111/j.1360-0443.2009.02564.x. PMID 19426289.
  4. ↑ Cuena Boy R, Maciá Martínez MA (1998). "[Extrapyramidal toxicity caused by metoclopramide and clebopride: study of voluntary notifications of adverse effects to the Spanish Drug Surveillance System]" (in Spanish). Atencion Primaria 21 (5): 289–95. PMID 9608114. Free full text
  5. ↑ Pilla M, Perachon S, Sautel F, Garrido F, Mann A, Wermuth CG, Schwartz JC, Everitt BJ, Sokoloff P. Selective inhibition of cocaine-seeking behaviour by a partial dopamine D3 agonist. Nature. 1999;400:371–375.
  6. ↑ Miles EW. The tryptophan synthase alpha 2 beta 2 complex. Cleavage of a flexible loop in the alpha subunit alters allosteric properties. J Biol Chem. 1991 Jun 15;266(17):10715-8. PMID:1904055
  7. ↑ Burkhard P, Dominici P, Borri-Voltattorni C, Jansonius JN, Malashkevich VN. Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase. Nat Struct Biol. 2001 Nov;8(11):963-7. PMID:11685243 doi:http://dx.doi.org/10.1038/nsb1101-963
  8. ↑ Miles EW. The tryptophan synthase alpha 2 beta 2 complex. Cleavage of a flexible loop in the alpha subunit alters allosteric properties. J Biol Chem. 1991 Jun 15;266(17):10715-8. PMID:1904055

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