| 1 | Author
| John Kamsteega, Jan Van Brederode, Gerrit Van Nigtevecht | Requires cookie* | | Title
| Campion (Silene dioica)  | | | Abstract
| An enzyme catalyzing the transfer of the rhamnosyl moiety of UDP-L-rhamnose to the 6 -hydro-xyl 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 sti mulated by the divalent metal ions Mg2+, Mn2+ and Co2+, and has a "true Km" value of 0.09 mM for UDP-L-rhamnose and 2.2 mM 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 rhamnosy-lation 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. | | |
Reference
| Z. Naturforsch. 35c, 249—257 (1980); received October 22 1979 | | |
Published
| 1980 | | |
Keywords
| Silene dioica, Caryophyllaceae, Anthocyanin Biosynthesis, Cyanidin-, Pelargonidin-glycosides, Glycosyltransferases, Genetic Control | | |
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| default:Reihe_C/35/ZNC-1980-35c-0249.pdf | | | Identifier
| ZNC-1980-35c-0249 | | | Volume
| 35 | |
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