Properties and genetic control of anthocyanin 5-O-glucosyltransferase in flowers ofPetunia hybrida

✍ Scribed by L. M. V. Jonsson; M. E. G. Aarsman; J. Diepen; P. Vlaming; N. Smit; A. W. Schram

• Publisher: Springer-Verlag
• Year: 1984
• Tongue: English
• Weight: 782 KB
• Volume: 160
• Category: Article
• ISSN: 0032-0935
• DOI: 10.1007/bf00393415

✦ Synopsis

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 gM), 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 Mg 2 § or Ca 2 § 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 5-0glucosyltransferase activity was correlated with the gene Anl, but not with the gene Gf.