1vid

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[[Image:1vid.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1vid| PDB=1vid | SCENE= }}
{{STRUCTURE_1vid| PDB=1vid | SCENE= }}
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'''CATECHOL O-METHYLTRANSFERASE'''
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===CATECHOL O-METHYLTRANSFERASE===
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==Overview==
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Catechol O-methyltransferase (COMT, EC 2.1.1.6) is important in the central nervous system because it metabolizes catecholamine neurotransmitters such as dopamine. The enzyme catalyses the transfer of the methyl group from S-adenosyl-L-methionine (AdoMet) to one hydroxyl group of catechols. COMT also inactivates catechol-type compounds such as L-DOPA. With selective inhibitors of COMT in combination with L-DOPA, a new principle has been realized in the therapy of Parkinson's disease. Here we solve the atomic structure of COMT to 2.0 A resolution, which provides new insights into the mechanism of the methyl transfer reaction. The co-enzyme-binding domain is strikingly similar to that of an AdoMet-dependent DNA methylase, indicating that all AdoMet methylases may have a common structure.
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The line below this paragraph, {{ABSTRACT_PUBMED_8127373}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 8127373 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8127373}}
==About this Structure==
==About this Structure==
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[[Category: Neurotransmitter degradation]]
[[Category: Neurotransmitter degradation]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:33:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:39:21 2008''

Revision as of 20:39, 28 July 2008

Image:1vid.png

Template:STRUCTURE 1vid

CATECHOL O-METHYLTRANSFERASE

Template:ABSTRACT PUBMED 8127373

About this Structure

1VID is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of catechol O-methyltransferase., Vidgren J, Svensson LA, Liljas A, Nature. 1994 Mar 24;368(6469):354-8. PMID:8127373

Page seeded by OCA on Mon Jul 28 23:39:21 2008

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