Common Identity of UDP-Glucose: Anthocyanidin 3-O-Glucosyltransferase and UDP-Glucose: Flavonol 3-O-Glucosyltransferase in Flowers of Petunia hybrida

Autor: Wilma E. Donker-Koopman, A. G. M. Gerats, Johan Bastiaannet, Mirjam E. G. Aarsman, AndréW. Schram, L. M. V. Jonsson
Rok vydání: 1984
Předmět:
Zdroj: Zeitschrift für Naturforschung C. 39:559-567
ISSN: 1865-7125
0939-5075
DOI: 10.1515/znc-1984-0609
Popis: In an attempt to distinguish between the UDP-glucose: flavonol 3-O-glucosyltransferase (3GT) and the UDP-glucose: anthocyanidin 3-O-glucosyltransferase in flower buds of Petunia hybrida, several properties of these activities were determined. The 3-glucosylation of anthocyanidin had a pH-activity optimum of 7.2, that of flavonol pH 9.2 to 9.5. Anthocyanidin 3GT activity was lowered in the presence of EDTA or β-mercaptoethanol, but this was due to an effect on the anthocyanidin substrate. The two 3-glucosylating activities were to a similar extent inhibited by an increasing ionic strength in the enzyme assay and showed an identical iso-electric point (5.2) as determined by chromatofocusing. Molecular weights were identical: 26000, 52000 or 78000 daltons as determined by gel-filtration. Antiserum raised against partially purified 3GT gave identical immunoprecipitation curves with flavonol 3GT and anthocyanidin 3GT. Special attention was given to the 3-O-glucosyltransferase in mutants with low levels of 3GT activity. These mutants are unable to form significant amounts of anthocyanins but contain wild- type amounts of flavonols. The enzyme of such mutants had the same iso-electric point and identical titration-curves with antiserum as the enzyme from wildtype plants. 3GT from wildtype or mutant plants glucosylated flavonols at higher rates than anthocyanidins.
Databáze: OpenAIRE