PMID: 751641Dec 1, 1978Paper

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

Biochemical Genetics
J KamsteegG van Nigtevecht

Abstract

An enzyme catalyzing the transfer of the glucosyl moiety of UDP-glucose to the 5-hydroxyl group of cyanidin-3-rhamnosyl-(1 leads to 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" values of 0.5 x 10(-3) M for UDP-glucose and 3.6 x 10(-3) M 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.

References

Dec 1, 1975·Analytical Biochemistry·J Chandrarajan, L Klein
Sep 1, 1957·Biochimica Et Biophysica Acta·J R FLORINI, C S VESTLING
Jul 3, 1962·Biochemical and Biophysical Research Communications·G A BARBER
Nov 1, 1963·Archives of Biochemistry and Biophysics·G A BARBER

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Citations

Sep 3, 2009·Journal of Agricultural and Food Chemistry·Katarzyna Lorenc-KukułaJan Szopa

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