EC Number   |
General Information |
Reference |
|---|
   2.1.1.240 | metabolism |
biosynthetic pathway of stilbene compound production from phenylalanine involving the enzyme, overview |
736024, 736807 |
| 2.1.1.240 | metabolism |
two resveratrol O-methyltransferase genes (sbOMT1 and sbOMT3) from Sorghum bicolor are capable of using resveratrol as a substrate that yields methylated analogues of resveratrol. The sbOMT3 O-methyltransferase catalyzes the A-ring specific 3,5-bis-O-methylation of resveratrol, which in turn yields pterostilbene (3,5-dimethoxy-4'-hydroxystilbene) in coexpression with a stilbene synthase from Arachis hypogaea. In addition, resveratrol O-methyltransferase sbOMT1, which has a potential as eugenol O-methyltransferase, predominantly catalyzes the resveratrol B-ring (4'-O-methylation), which yields 3,5-dihydroxy-4'-methoxystilbene |
735842 |
| 2.1.1.240 | more |
three-dimensional enzyme homology modeling and docking study for identification of four key catalytic residues. Residues F167 and W258 form a sandwich to bind resveratrol, residue D174 is in close proximity to the substrate, and residue H261 might serve as a general base in the deprotonation of hydroxyl groups |
735437 |
| 2.1.1.240 | physiological function |
synthesis mechanism of pterostilbene in case of Geotrichum citriaurantii infection, and regulation of resveratrol O-methyltransferase gene in pterostilbene defensing the sour rot (Geotrichum citriaurantii) of wine grape, overview. Pterostilbene, the most important phytoalexin, effectively inhibits the activity of Geotrichum citriaurantii |
757339 |
| 2.1.1.240 | physiological function |
the multifunctional caffeic acid O-methyltransferase (COMT, EC 2.1.1.46) originating from Arabidopsis thaliana also catalyzes the transfer of a methyl group to resveratrol resulting in pterostilbene production (EC 2.1.1.240) |
757597 |
