Properties and genetic control of anthocyanin 5-O-glucosyltransferase in flowers of Petunia hybrida |
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Authors: | L M V Jonsson M E G Aarsman J van Diepen P de Vlaming N Smit A W Schram |
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Affiliation: | (1) Research Section Biosynthesis of Flavonoids , Department of Plant Physiology, University of Amsterdam, Kruislaan 318, NL-1098 SM Amsterdam, The Netherlands;(2) Department of Genetics, University of Amsterdam, Kruislaan 318, NL-1098 SM Amsterdam, The Netherlands |
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Abstract: | An anthocyanin 5-O-glucosyltransferase from flowers of Petunia hybrida was purified about 30-fold. Using uridine 5 -diphosphoglucose as glucose donor (Km 0.22 mM), the enzyme glucosylated the 3-(p-coumaroyl)-rutinoside derivatives of delphinidin and petunidin (Km 3 M), isolated from pollen of Petunia. Delphinidin 3-rutinoside, cyanidin 3-rutinoside and delphinidin 3-glucoside did not serve as substrates. The glucosylation of petunidin 3-(p-coumaroyl)-rutinoside showed a pH-activity optimum at pH 8.3 and was neither stimulated by Mg2+ or Ca2+, nor inhibited by ethylenediaminetetraacetic acid. After separating the 5-O-glucosyltransferase from the anthocyanidin 3-O-glucosyltransferase by means of chromatofocusing, it was shown that both enzymes exhibit a high degree of positional specificity. The 5-O-glucosyltransferase activity was correlated with the gene An1, but not with the gene Gf.Abbreviations HPLC
high performance liquid chromatography
- 3GT
3-O-glucosyltransferase
- 5GT
5-O-glucosyltransferase
- 3RGac
3-(p-coumaroyl)-rutinoside
- 3RGac5G
3-(p-coumaroyl)-rutinoside-5-glucoside
- UDPGlc
uridine 5 -diphosphoglucose |
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Keywords: | Anthocyanim biosynthesis Anthocyanin glucosyltransferase Anthocyanidin 3-(p-coumaroyl)-rutinoside Kelunia |
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