Cloning and characterization of Vitis vinifera UDP-glucose:flavonoid 3-O-glucosyltransferase, a homologue of the enzyme encoded by the maize Bronze-1 locus that may primarily serve to glucosylate anthocyanidins in vivo.

The Journal of Biological Chemistry
C M FordP B Hoj

Abstract

We report here the cloning and optimized expression at 16 degrees C and the characterization of a Vitis vinifera UDP-glucose:flavonoid 3-O-glucosyltransferase, an enzyme responsible for a late step in grapevine anthocyanin biosynthesis. The properties of this and other UDP-glucose:flavonoid 3-O-glucosyltransferases, homologues of the product encoded by the maize Bronze-1 locus, are a matter of conjecture. The availability of a purified recombinant enzyme allowed for the unambiguous determination of the characteristics of a flavonoid 3-O-glucosyltransferase. Kinetic analyses showed that kcat for glucosylation of cyanidin, an anthocyanidin substrate, is 48 times higher than for glucosylation of the flavonol quercetin, whereas Km values are similar for both substrates. Activity toward other classes of substrates is absent. Cu2+ ions strongly inhibit the action of this and other glucosyltransferases; however, we suggest that this phenomenon in large part is due to Cu2+-mediated substrate degradation rather than inhibition of the enzyme. Additional lines of complementary biochemical data also indicated that in the case of V. vinifera, the principal, if not only, role of UDP-glucose:flavonoid 3-O-glucosyltransferases is to glucosylat...Continue Reading

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Citations

May 12, 2010·Planta·Takashi Nakatsuka, Masahiro Nishihara
Jul 7, 2012·Glycoconjugate Journal·Guangxiang RenPeng George Wang
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Oct 20, 2005·Journal of Bioscience and Bioengineering·T KokuboT Kodama
Apr 27, 2012·Journal of Agricultural and Food Chemistry·Alessandra FerrandinoAndrea Schubert
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Jun 16, 2009·Plant Physiology·Philippe HugueneyAgnès Ageorges
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Sep 14, 2013·International Journal of Molecular Sciences·António TeixeiraHernâni Gerós
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