In flower extracts of defined genotypes of Matthiola incana, an enzyme was demonstrated which catalyzes the transfer of the glucosyl moiety of uridine 5'-diphosphoglucose (UDPGlc) to the 5-hydroxyl group of pelargonidin and cyanidin 3-glycosides and acylated derivatives. The best substrate for 5-glu
Purification and characterization of UDP-glucose: anthocyanin 3′,5′-O-glucosyltransferase fromClitoria ternatea
✍ Scribed by Koichiro Kogawa; Naoki Kato; Kohei Kazuma; Naonobu Noda; Masahiko Suzuki
- Publisher
- Springer-Verlag
- Year
- 2007
- Tongue
- English
- Weight
- 452 KB
- Volume
- 226
- Category
- Article
- ISSN
- 0032-0935
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An enzyme catalyzing the transfer of the glucosyl moiety of UDP-glucose to the 3-hydroxyl group of cyanidin has been demonstrated in petal extracts of Silene dioica mutants with cyanidin-3-O-glucoside in the petals. This transferase activity was also present in young rosette leaves and calyces of th
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 e