Properties and genetic control of anthocyanin 5-O-glucosyltransferase in flowers of Petunia hybrida View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1984-03

AUTHORS

L. M. V. Jonsson, M. E. G. Aarsman, J. van Diepen, P. de Vlaming, N. Smit, A. W. Schram

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 μM), 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-O-glucosyltransferase activity was correlated with the gene An1, but not with the gene Gf. More... »

PAGES

341-347

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00393415

DOI

http://dx.doi.org/10.1007/bf00393415

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1026158183

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24258583


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