EC Number   |
Inhibitors |
Structure  |
|---|
   2.1.1.6 | more |
inhibition by analogs of S-adenosyl-homcysteine |
 |
| 2.1.1.6 | more |
relationship between the structure of flavonoids and their inhibitory activity |
|
| 2.1.1.6 | more |
substrate inhibition is dependent on the concentration of S-adenosylmethionine and MgCl2 |
|
| 2.1.1.6 | more |
activity of the enzyme is strongly influenced by the nature of the buffer |
|
| 2.1.1.6 | more |
no inhibition by genistein, daidzein and biochanin A |
|
| 2.1.1.6 | more |
role of COMT inhibitors in Parkinsons disease as a new therapeutic approach to Parkinsons disease involving conversion of levodopa to dopamine at the target region in the brain and facilitation of the continuous action of this amine at the receptor sites. A historical overview of the discovery and development of COMT inhibitors is presented with a special emphasis on nebicapone, presently under clinical development, as well as entacapone and tolcapone, which are already approved as adjuncts in the therapy of Parkinsons disease. This article reviews human pharmacokinetic and pharmacodynamic properties of these drugs as well as their clinical efficacy and safety |
|
| 2.1.1.6 | more |
COMT is a target for inhibitor development aiming at Parkinsons disease treatment and is submitted to extensive structure-based drug design |
|
| 2.1.1.6 | more |
(-)-epigallocatechin is not active even at a concentration of 0.05 mM |
|
| 2.1.1.6 | more |
COMT activity appears unaffected by loss of the dopaminergic nigrostriatal pathway and levodopa treatment |
|
| 2.1.1.6 | Mg2+ |
inhibition above 2 mM; required for activity |
  |
