Summary
In extracts of petals of M. album, an enzyme has been demonstrated which catalyzes the transfer of the glucosyl moiety of UDP-glucose to the 7-hydroxylgroup of isovitexin.
This enzyme is controlled by a dominant gene G; in plants with the recessive genotype no glucosyltransferase activity could be detected.
The enzyme was purified 16-fold by (NH4)2SO4 fractionation and Sephadex-chromatography.
The glucosyltransferase had a pH optimum of pH 7.5, was not stimulated by divalent metal ions, and had a “true Km” value of 1.2x10-4 M for UDP-glucose and a “true Km” value of 4.6x10-4 M for isovitexin.
Several flavones with an apigenin hydroxylation pattern could serve as glucosyl acceptors. The highest activity was found, however, with isovitexin.
The enzyme was unable to catalyze the transfer of xylose from UDP-xylose to the 7-hydroxylgroup of isovitexin, although isovitexin 7-O-xyloside has been found in petals of M. album plants.
ADP-glucose could not serve as a glucosyl donor.
The transferase activity was also present in leaves and calyces of GG plants. In these organs the transferase uses another flavone as a substrate. Neither isovitexin 7-O-glucoside nor isovitexin could be detected in these organs.
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van Brederode, J., van Nigtevecht, G. Identification, properties and genetic control of UDP-glucose: Isovitexin 7-O-glucosyltransferase isolated from petals of Melandrium album . Molec. Gen. Genet. 122, 215–229 (1973). https://doi.org/10.1007/BF00278598
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DOI: https://doi.org/10.1007/BF00278598