Biochemical Genetics

, Volume 16, Issue 11, pp 1059–1071

Identification, properties, and genetic control of UDP-glucose: Cyanidin-3-rhamnosyl-(1→6)-glucoside-5-O-glucosyltransferase isolated from petals of the red campion (Silene dioica)

  • John Kamsteeg
  • Jan van Brederode
  • Gerrit van Nigtevecht
Article

DOI: 10.1007/BF00484526

Cite this article as:
Kamsteeg, J., van Brederode, J. & van Nigtevecht, G. Biochem Genet (1978) 16: 1059. doi:10.1007/BF00484526

Abstract

An enzyme catalyzing the transfer of the glucosyl moiety of UDP-glucose to the 5-hydroxyl group of cyanidin-3-rhamnosyl-(1→6)-glucoside has been demonstrated in petal extracts of Silene dioica plants. This glucosyltransferase activity was not detectable in green parts of these plants. The enzyme activity is controlled by a single dominant gene M; no glucosyltransferase activity could be demonstrated in petals of m/m plants. The enzyme was purified eightyfold by PVP and Sephadex G50 chromatography. The glucosyltransferase had a pH optimum of 7.4, had a molecular weight of about 55,000, was stimulated by divalent metal ions, and had a “true Km” value of 0.5×10−3m for UDP-glucose and 3.6×10−3m for cyanidin-3-rhamnosylglucoside. Pelargonidin-3-rhamnosylglucoside also could serve as acceptor. The enzyme did not catalyze the glucosylation of the 5-hydroxyl group of cyanidin-3-glucoside, although in petals of M/- n/n mutants cyanidin-3,5-diglucoside is present. ADP-glucose could not serve as a glucosyl donor.

Key words

Silene dioicaCaryophyllaceaeRed Campionanthocyanin biosynthesisglycosylation5-O-glucosyltransferasegenetic controlcyanidin and pelargonidin glycosides

Copyright information

© Plenum Publishing Corporation 1978

Authors and Affiliations

  • John Kamsteeg
    • 1
  • Jan van Brederode
    • 1
  • Gerrit van Nigtevecht
    • 1
  1. 1.Department of Population and Evolutionary BiologyUniversity of UtrechtUtrechtThe Netherlands