Enzymes
| UniProtKB help_outline | 3 proteins |
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-galactose Identifier CHEBI:66914 Charge -2 Formula C15H22N2O17P2 InChIKeyhelp_outline HSCJRCZFDFQWRP-ABVWGUQPSA-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 105 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-galactoside Identifier CHEBI:77935 Charge -1 Formula C21H19O11 InChIKeyhelp_outline RKWHWFONKJEUEF-WVXKDWSHSA-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 2 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:35631 | RHEA:35632 | RHEA:35633 | RHEA:35634 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline | ||||
| Gene Ontology help_outline | ||||
| KEGG help_outline | ||||
| MetaCyc help_outline |
Publications
-
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.
-
Purification and characterization of glycosyltransferases involved in anthocyanin biosynthesis in cell-suspension cultures of Daucus carota L.
Rose A., Glassgen W.E., Hopp W., Seitz H.U.
The major anthocyanins accumulated by an Afghan cultivar of Daucus carota L. are cyanidin 3-(xylosylglucosylgalactosides) acylated with sinapic or ferulic acid. The formation of the branched triglycoside present as a common structural element requires an ordered sequence of glycosylation events. T ... >> More
The major anthocyanins accumulated by an Afghan cultivar of Daucus carota L. are cyanidin 3-(xylosylglucosylgalactosides) acylated with sinapic or ferulic acid. The formation of the branched triglycoside present as a common structural element requires an ordered sequence of glycosylation events. Two of these enzymic glycosylation reactions have been detected in protein preparations from carrot cell-suspension cultures. The first step is a galactosyl transfer catalyzed by UDP-galactose: cyanidin galactosyltransferase (CGT) resulting in cyanidin 3-galactoside. The putative second step is the formation of cyanidin 3-(xylosylgalactoside) catalyzed by UDP-xylose: cyanidin 3-galactoside xylosyltransferase (CGXT). Both enzyme activities were characterized from crude protein preparations. The CGT was purified 526-fold from the cytosolic fraction of UV-irradiated cell cultures by ion-exchange chromatography on diethylaminoethyl (DEAE)-Sephacel, affinity chromatography on Blue Sepharose CL-6B, gel permeation chromatography on Sephadex G-75 and elution from the gel matrix after non-dissociating PAGE. Its molecular mass was estimated by SDS-PAGE and by calibrated gel permeation chromatography on Sephadex G-75. In both cases a molecular mass of 52 kDa was determined, indicating that the native protein is a monomer of 52 kDa. The galactosyl transfer and the xylosyl transfer are presumed to be catalyzed by separate enzymes. << Less
Planta 198:397-403(1996) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.