Structural highlights
Function
FAOMT_VITVI Mediates O-methylation of anthocyanins. Anthocyanins are major pigments in grapes: at ripening initiation in red grapevine berries, the exocarp turns color from green to red and then to purple due to the accumulation and extent of methylation of anthocyanins. Catalyzes both 3' and 5' O-methylation of anthocyanins, with a preference for glycosylated substrates. Active on both anthocyanins and flavonols in vitro. Most active with delphinidin 3-glucoside but also acts on cyanidin 3-glucoside, cyanidin, myricetin, quercetin and quercetin 3-glucoside. Not able to methylate flavan type skeletons with chiral centers, such as catechins or dihydroquercetin.[1] [2]
References
- ↑ Hugueney P, Provenzano S, Verriès C, Ferrandino A, Meudec E, Batelli G, Merdinoglu D, Cheynier V, Schubert A, Ageorges A. A novel cation-dependent O-methyltransferase involved in anthocyanin methylation in grapevine. Plant Physiol. 2009 Aug;150(4):2057-70. PMID:19525322 doi:10.1104/pp.109.140376
- ↑ Lücker J, Martens S, Lund ST. Characterization of a Vitis vinifera cv. Cabernet Sauvignon 3',5'-O-methyltransferase showing strong preference for anthocyanins and glycosylated flavonols. Phytochemistry. 2010 Sep;71(13):1474-84. PMID:20580386 doi:10.1016/j.phytochem.2010.05.027