Catechol O-methyltransferase

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== Function ==
== 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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'''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.<ref>PMID:19111934</ref>
== Relevance ==
== 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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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:25559423</ref>
==Structural highlights ==
==Structural highlights ==

Revision as of 09:08, 6 December 2015

Structure of human catechol O-methyltransferase complex with SAM and dinitrocatechol (PDB entry 3a7e)

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3D Structures of catechol O-methyltransferase

Updated on 06-December-2015

References

  1. 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
  2. Muller T. Catechol-O-methyltransferase inhibitors in Parkinson's disease. Drugs. 2015 Feb;75(2):157-74. doi: 10.1007/s40265-014-0343-0. PMID:25559423 doi:http://dx.doi.org/10.1007/s40265-014-0343-0

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Michal Harel, Alexander Berchansky

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