Enzymes
| UniProtKB help_outline | 6 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
- Name help_outline cyanidin Identifier CHEBI:71682 Charge -1 Formula C15H9O6 InChIKeyhelp_outline VEVZSMAEJFVWIL-UHFFFAOYSA-M SMILEShelp_outline Oc1cc([O-])c2cc([O-])c([o+]c2c1)-c1ccc(O)c(O)c1 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP-α-D-glucose Identifier CHEBI:58885 (Beilstein: 3827329) help_outline Charge -2 Formula C15H22N2O17P2 InChIKeyhelp_outline HSCJRCZFDFQWRP-JZMIEXBBSA-L SMILEShelp_outline OC[C@H]1O[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2ccc(=O)[nH]c2=O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 231 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline cyanidin 3-O-β-D-glucoside Identifier CHEBI:77857 Charge -1 Formula C21H19O11 InChIKeyhelp_outline RKWHWFONKJEUEF-GQUPQBGVSA-M SMILEShelp_outline OC[C@H]1O[C@@H](Oc2cc3c([O-])cc([O-])cc3[o+]c2-c2ccc(O)c(O)c2)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP Identifier CHEBI:58223 Charge -3 Formula C9H11N2O12P2 InChIKeyhelp_outline XCCTYIAWTASOJW-XVFCMESISA-K SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])(=O)OP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 576 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:60100 | RHEA:60101 | RHEA:60102 | RHEA:60103 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Molecular cloning and biochemical characterization of the UDP-glucose: flavonoid 3-O-glucosyltransferase from Concord grape (Vitis labrusca).
Hall D., Yuan X.X., Murata J., De Luca V.
Glucosylation of anthocyanidin substrates at the 3-O-position is crucial for the red pigmentation of grape berries and wine. The gene that encodes the enzyme involved in this reaction has been cloned from Vitis labrusca cv. Concord, heterologously expressed, and the recombinant enzyme (rVL3GT) was ... >> More
Glucosylation of anthocyanidin substrates at the 3-O-position is crucial for the red pigmentation of grape berries and wine. The gene that encodes the enzyme involved in this reaction has been cloned from Vitis labrusca cv. Concord, heterologously expressed, and the recombinant enzyme (rVL3GT) was characterized. VL3GT has 96% amino acid sequence identity with Vitis vinifera VV3GT and groups phylogenetically with several other flavonoid 3-O-glycosyltransferases. In vitro substrate specificity studies and kinetic analyses of rVL3GT indicate that this enzyme preferentially glucosylates cyanidin as compared with quercetin. Crude protein extracts from several Concord grape tissues were assayed for glucosyltransferase activity with cyanidin and quercetin as acceptor substrates. A comparison of the VL3GT activities toward with these substrates showed that the 3GT enzyme activity is consistent with the expression of VL3GT in these tissues and is coincident with the biosynthesis of anthocyanins in both location and developmental stages. Enzyme activities in grape mesocarp, pre-veraison exocarp, leaf, flower bud, and flower tissues glucosylated quercetin but not cyanidin at high rates, suggesting the presence of additional enzymes which are able to glucosylate the 3-O-position of flavonols with higher specificity than anthocyanidins. << Less
Phytochemistry 74:90-99(2012) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Characterization of two key flavonoid 3-O-glycosyltransferases involved in the formation of flower color in Rhododendron delavayi.
Sun W., Sun S., Xu H., Wang Y., Chen Y., Xu X., Yi Y., Ju Z.
Flower color, largely determined by anthocyanin, is one of the most important ornamental values of <i>Rhododendron delavayi</i>. However, scant information of anthocyanin biosynthesis has been reported in <i>R. delavayi</i>. We found that anthocyanidin 3-<i>O</i>-glycosides were the predominant an ... >> More
Flower color, largely determined by anthocyanin, is one of the most important ornamental values of <i>Rhododendron delavayi</i>. However, scant information of anthocyanin biosynthesis has been reported in <i>R. delavayi</i>. We found that anthocyanidin 3-<i>O</i>-glycosides were the predominant anthocyanins detected in <i>R. delavayi</i> flowers accounting for 93.68-96.31% of the total anthocyanins during its development, which indicated the key role of flavonoid 3-<i>O</i>-glycosyltransferase (3GT) on <i>R. delavayi</i> flower color formation. Subsequently, based on correlation analysis between anthocyanins accumulation and <i>Rd3GTs</i> expressions during flower development, <i>Rd3GT1</i> and <i>Rd3GT6</i> were preliminarily identified as the pivotal <i>3GT</i> genes involved in the formation of color of <i>R. delavayi</i> flower. Tissue-specific expressions of <i>Rd3GT1</i> and <i>Rd3GT6</i> were examined, and their function as 3GT <i>in vivo</i> was confirmed through introducing into <i>Arabidopsis UGT78D2</i> mutant and <i>Nicotiana tabacum</i> plants. Furthermore, biochemical characterizations showed that both <i>Rd3GT1</i> and <i>Rd3GT6</i> could catalyze the addition of UDP-sugar to the 3-OH of anthocyanidin, and preferred UDP-Gal as their sugar donor and cyanidin as the most efficient substrate. This study not only provides insights into the biosynthesis of anthocyanin in <i>R. delavayi</i>, but also makes contribution to understand the mechanisms of its flower color formation. << Less
Front. Plant Sci. 13:863482-863482(2022) [PubMed] [EuropePMC]
This publication is cited by 10 other entries.
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Identification and properties of UDP-glucose: cyanidin-3-O-glucosyltransferase isolated from petals of the red campion (Silene dioica).
Kamsteeg J., van Brederode J., van Nigtevecht G.
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 ... >> More
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 these plants. The highest glucosyltransferase activity was found in petals of opening flowers of young plants. The enzyme was purified ninetyfold by PVP and Sephadex chromatography. The glucosyltransferase had a pH optimum of 7.5, had a "true Km value" of 4.1 x 10(-4) M for UDP-glucose and 0.4 x 10(-4) M for cyanidin chloride, and was not stimulated by divalent metal ions. Both p-chloromercuribenzoate and HgCl2 inhibited the enzyme activity. Pelargonidin chloride and delphinidin chloride at reduced rates also served as substrates. The enzyme did not catalyze the glucosylation of the 3-hydroxyl group of flavonols or the 5-hydroxyl group of anthocyanins. ADP-glucose could not serve as a glucosyl donor. The results of Sephadex G150 chromatography suggest that the glucosyltransferase can exist as dimer of about 125,000 daltons and as active monomers of 60,000 daltons. The genetic control of the glucosyltransferase activity is discussed. << Less
Biochem Genet 16:1045-1058(1978) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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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.
Ford C.M., Boss P.K., Hoj P.B.
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-gl ... >> More
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 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. << Less
J. Biol. Chem. 273:9224-9233(1998) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.