Catechol-O-Methyltransferase
- OMIM: 116790
- UniProt: P21964
Catechol-O- methyltransferase ( gene: COMT ) is called the one enzyme that various catecholamines, including natural neurotransmitters and neuroactive drugs, O- methylated and thus inactivated and mining supplies. It is thus part of the catecholamine depletion and xenobiotic metabolism. COMT is found in all living organisms and is especially expressed in the brain, liver and placenta, as well as in lymphocytes and erythrocytes. In humans, there are two isoforms of COMT: MB- COMT is membrane-bound and S- COMT ( lacking the first 50 amino acids) to move freely.
COMT was discovered by U.S. biochemist Julius Axelrod.
Function
COMT disabled, especially in the sympathetic nerve endings of noradrenaline, adrenaline and dopamine. The inactivation of this neurotransmitter occurs by transfer of a methyl group from S- adenosylmethionine (SAM ) to a phenolic hydroxyl group by the catechol-O- methyltransferase, to which the oxidative deamination by monoamine oxidase (MAO ) is connected.
The COMT inhibiting - also by methylation - also various drugs, the compounds used in the treatment of Parkinson's disease levodopa and dopamine. To turn this deactivation, COMT inhibitors have been developed.
Pathology
COMT polymorphism, so the occurrence of genetic variants are associated with a number of mental changes such as anxiety and schizophrenia, but also especially eating disorders and obesity. These relationships, as well as the role of COMT in the processing of pain, are currently being explored. The results for schizophrenia are contradictory.
Environmental toxins, but also the soy ingredients daidzein and genistein, the COMT can block and thus contribute to the accumulation of degradation products with the following damage to the organism.
In a retrospective study, it was shown that patients often suffer with a reduced COMT activity a shock in bypass operations and have a higher mortality risk during surgery.
Pre-eclampsia is associated with COMT deficiency.