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An enzyme catalyzing the transfer of the rhamnosyl moiety of UDP-ʟ-rhamnose to the 6 -hydroxyl group of the 3-O-bound glucose of anthocyanidin 3-O-glucosides has been demonstrated in petal extracts of Silene dioica plants. The enzyme activity is controlled by a single dominant gene N; no rhamnosyltransferase activity is found in petals of n/n plants. The 60-fold purified rhamno-syltransferase exhibits a pH optimum of 8.1, has a molecular weight of about 45000 daltons, is stimulated by the divalent metal ions Mg 2+ , Mn 2+  and Co 2+ , and has a “true Km” value of 0.09 mᴍ for UDP-ʟ-rhamnose and 2.2 mᴍ for cyanidin 3-O-glucoside. Pelargonidin 3-O-glucoside and delphinidin 3-O-glucoside can also serve as acceptor. The enzyme can also catalyze the rhamnosylation of anthocyanidin 3,5-diglucosides although at reduced rate. The biosynthetic pathway for the synthesis of cyanidin 3-rhamnosylglucoside-5-glucoside in petals of S. dioica is discussed.

zeitschrift für naturforschung c

Identification, Properties and Genetic Control of UDP-ʟ-Rhamnose: Anthocyanidin 3-O-Glucoside, 6″-O-Rhamnosyltransferase Isolated from Retals of the Red Campion (Silene dioica)