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	additional information	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