Catechol O-methyltransferase
From Proteopedia
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<StructureSection load='3a7e' size='450' side='right' caption='Structure of human catechol O-methyltransferase complex with SAM and dinitrocatechol (PDB entry [[3a7e]])' scene='55/551215/Cv/1'> | <StructureSection load='3a7e' size='450' side='right' caption='Structure of human catechol O-methyltransferase complex with SAM and dinitrocatechol (PDB entry [[3a7e]])' scene='55/551215/Cv/1'> | ||
| + | == Function == | ||
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| + | '''Catechol O-methyltransferase''' (COMT) methylates catecholamines like dopamine, epinephrine and norepinephrine. The cofactor S-adenosyl-L-methionine (SAM) serves as the methyl donor in the reaction and is converted to to S-adenosyl-L-homocysteine (SAH) by the reaction. | ||
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| + | == Relevance == | ||
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| + | The Parkinson Disease drug levodopa is a substrate of COMT and COMT inhibitors like entacapone are used with levodopa in the disease treatment.<ref>PMID:19111934</ref> | ||
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| + | ==Structural highlights == | ||
| - | '''Catechol O-methyltransferase''' (COMT) methylates catecholamines like dopamine, epinephrine and norepinephrine. The cofactor S-adenosyl-L-methionine (SAM) serves as the methyl donor in the reaction and is converted to to S-adenosyl-L-homocysteine (SAH) by the reaction. The Parkinson Disease drug levodopa is a substrate of COMT and COMT inhibitors like entacapone are used with levodopa in the disease treatment.<ref>PMID:19111934</ref> | ||
*<scene name='55/551215/Cv/2'>Active site of human catechol O-methyltransferase complex with SAM and dinitrocatechol</scene> (PDB entry [[3a7e]]). | *<scene name='55/551215/Cv/2'>Active site of human catechol O-methyltransferase complex with SAM and dinitrocatechol</scene> (PDB entry [[3a7e]]). | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:49, 23 November 2015
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3D Structures of catechol O-methyltransferase
Updated on 23-November-2015
References
- ↑ Tsuji E, Okazaki K, Isaji M, Takeda K. Crystal structures of the Apo and Holo form of rat catechol-O-methyltransferase. J Struct Biol. 2008 Dec 10. PMID:19111934 doi:S1047-8477(08)00293-1
