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1980 (1)
1Author    John Kamsteega, Jan Van Brederode, Gerrit Van NigtevechtRequires 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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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0249.pdf 
 Identifier    ZNC-1980-35c-0249 
 Volume    35