1h1d
From Proteopedia
(New page: 200px<br /> <applet load="1h1d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h1d, resolution 2.0Å" /> '''CATECHOL O-METHYLTRA...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1H1D is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]] with MG, SAM and BIA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.6 2.1.1.6]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H1D OCA]]. | + | 1H1D is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]] with MG, SAM and BIA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Catechol_O-methyltransferase Catechol O-methyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.6 2.1.1.6]]. Structure known Active Site: MG1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H1D OCA]]. |
==Reference== | ==Reference== | ||
Kinetics and crystal structure of catechol-o-methyltransferase complex with co-substrate and a novel inhibitor with potential therapeutic application., Bonifacio MJ, Archer M, Rodrigues ML, Matias PM, Learmonth DA, Carrondo MA, Soares-Da-Silva P, Mol Pharmacol. 2002 Oct;62(4):795-805. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12237326 12237326] | Kinetics and crystal structure of catechol-o-methyltransferase complex with co-substrate and a novel inhibitor with potential therapeutic application., Bonifacio MJ, Archer M, Rodrigues ML, Matias PM, Learmonth DA, Carrondo MA, Soares-Da-Silva P, Mol Pharmacol. 2002 Oct;62(4):795-805. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12237326 12237326] | ||
| + | [[Category: Catechol O-methyltransferase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: neurotransmitter degradation]] | [[Category: neurotransmitter degradation]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:07:15 2007'' |
Revision as of 09:02, 30 October 2007
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CATECHOL O-METHYLTRANSFERASE
Overview
Catechol-O-methyltransferase (COMT; E.C. 2.1.1.6) is a ubiquitous enzyme, in nature that plays an important role in the metabolism of catechol, neurotransmitters and xenobiotics. In particular, inactivation of drugs, such as L-3,4-dihydroxyphenylalanine (L-DOPA) via O-methylation is of, relevant pharmacological importance, because L-DOPA is currently the most, effective drug used in the treatment of Parkinson's disease. This, justified the interest in developing COMT inhibitors as potential adjuncts, to L-DOPA therapy. The kinetics of inhibition by BIA 3-335, (1-[3,4-dihydroxy-5-nitrophenyl]-3-(N-3'-trifluormethylphenyl)-piperazine-, 1-propanone dihydrochloride) were characterized using recombinant rat, soluble COMT. BIA 3-335 was found to act as a potent, reversible, tight-binding ... [(full description)]
About this Structure
1H1D is a [Single protein] structure of sequence from [Rattus norvegicus] with MG, SAM and BIA as [ligands]. Active as [Catechol O-methyltransferase], with EC number [2.1.1.6]. Structure known Active Site: MG1. Full crystallographic information is available from [OCA].
Reference
Kinetics and crystal structure of catechol-o-methyltransferase complex with co-substrate and a novel inhibitor with potential therapeutic application., Bonifacio MJ, Archer M, Rodrigues ML, Matias PM, Learmonth DA, Carrondo MA, Soares-Da-Silva P, Mol Pharmacol. 2002 Oct;62(4):795-805. PMID:12237326
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