catechol-o-methyl transferase

(redirected from Catechol-o-methyltransferase)

catechol-o-methyl transferase (COMT)

[kat′əkol′ōmeth′il]
an enzyme that deactivates the catecholamines dopa, dopamine, epinephrine, and norepinephrine.

catechol-o-methyl transferase (COMT),

n an enzyme that deactivates epinephrine and norepinephrine.
References in periodicals archive ?
Opicapone, an investigational drug in the US, is a once-daily, peripherally-acting, highly-selective catechol-o-methyltransferase (COMT) inhibitor being developed as an adjunct therapy to preparations of levodopa/DOPA decarboxylase inhibitors for adult patients with Parkinson's disease and motor fluctuations.
Currently, pharmacological treatment of motor symptoms of PD depends mainly on the administration of dopaminergic drugs (levodopa and dopamine agonists) and other drugs involved in levodopa metabolism (monoamine oxidase-B inhibitors and catechol-O-methyltransferase inhibitors).
Researchers are now discovering that the activity of an enzyme called catechol-O-methyltransferase, which is encoded by the COMT gene, may explain why some people are more resilient to stress than others.
Catechol-O-methyltransferase inhibitors (COMT inhibitors) These are prescribed for people in later stages of Parkinson's disease.
Meta-analysis of association between a catechol-O-methyltransferase gene polymorphism and attention deficit hyperactivity disorder.
The study suggested that common genetic variation in the gene for catechol-O-methyltransferase (COMT) might modify the cardiovascular benefit of aspirin and in some people it might confer slight harm.
Catechol-O-methyltransferase (COMT) plays a particularly crucial role in the regulation of prefrontal DA turnover.
In particular, prefrontal functions are influenced by polymorphism of the gene coding for catechol-O-methyltransferase (COMT).
Dopamine is metabolized by catechol-O-methyltransferase into methoxytyramine within head and neck paragangliomas (HNPGL).
Functional maternal catechol-O-methyltransferase polymorphism and fetal growth restriction.
Catechol-O-methyltransferase (COMT) enzyme which is principally responsible for both the inactivation and detoxification of carcinogenic catechol estrogens.
The presence of caffeic acid or chlorogenic acid inhibited DNA methylation predominantly through a non-competitive mechanism, and this inhibition was largely due to the increased formation of S-adenosyl-L-homocysteine (SAH, a potent inhibitor of DNA methylation), resulting from the catechol-O-methyltransferase (COMT)-mediated O-methylation of these dietary catechols.