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

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dc.contributor.authorFord, C.
dc.contributor.authorBoss, P.
dc.contributor.authorHoj, P.
dc.date.issued1998
dc.description.abstractWe report here the cloning and optimized expression at 16 °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-1locus, 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 k cat for glucosylation of cyanidin, an anthocyanidin substrate, is 48 times higher than for glucosylation of the flavonol quercetin, whereasK m 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 glucosylate anthocyanidins in red fruit during ripening. Other glucosyltransferases with a much higher relative activity toward quercetin are suggested to glucosylate flavonols in a distinct spatial and temporal pattern. It should be considered whether gene products homologous to Bronze-1 in some cases more accurately should be referred to as UDP-glucose:anthocyanidin 3-O-glucosyltransferases.
dc.description.statementofresponsibilityChristopher M. Ford, Paul K. Boss, and Peter Bordier Høj
dc.identifier.citationJournal of Biological Chemistry, 1998; 273(15):9224-9233
dc.identifier.doi10.1074/jbc.273.15.9224
dc.identifier.issn1083-351X
dc.identifier.issn1083-351X
dc.identifier.orcidFord, C. [0000-0003-1617-2977]
dc.identifier.orcidBoss, P. [0000-0003-0356-9342]
dc.identifier.urihttp://hdl.handle.net/2440/13048
dc.language.isoen
dc.publisherAmerican Society for Biochemistry and Molecular Biology
dc.rights© 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
dc.source.urihttps://doi.org/10.1074/jbc.273.15.9224
dc.subjectZea mays
dc.subjectRosales
dc.subjectCopper
dc.subjectAnthocyanins
dc.subjectGlucosyltransferases
dc.subjectRecombinant Proteins
dc.subjectDNA Primers
dc.subjectCloning, Molecular
dc.subjectPolymerase Chain Reaction
dc.subjectSequence Alignment
dc.subjectAmino Acid Sequence
dc.subjectSequence Homology, Amino Acid
dc.subjectSubstrate Specificity
dc.subjectGlycosylation
dc.subjectKinetics
dc.subjectGenes, Plant
dc.subjectMolecular Weight
dc.subjectMolecular Sequence Data
dc.titleCloning 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
dc.typeJournal article
pubs.publication-statusPublished

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