A UDP-Glucose:Isoflavone 7-O-Glucosyltransferase from the Roots of Soybean (Glycine max) Seedlings

Niimi, Akio; Saito, Atsushi; Homma, Yoshio; Nakao, Masahiro; Sasaki, Nobuhiro; Nishino, Tokuzo; Takahashi, Shigetoshi; Nakayama, Tôru

doi:10.1074/jbc.m702651200

Cited by 122 publications

(71 citation statements)

References 38 publications

(59 reference statements)

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“…The enzyme displayed high k cat values for quercetin and kaempferol, which were 10-to 100-fold higher than the values reported for many other UGTs at optimal pH (e.g., Noguchi et al, 2007).…”

Section: Biochemical Characterization Of Vv Gt5 and Vv Gt6mentioning

confidence: 54%

Section: Biochemical Characterization Of Vv Gt5 and Vv Gt6mentioning

confidence: 87%

“…The enzymatic reaction followed Michaelis-Menten kinetics, and the steady state kinetic parameters were determined at pH 9.1 and 308C as summarized in Table 2. The enzyme displayed high k cat values for quercetin and kaempferol, which were 10-to 100-fold higher than the values reported for many other UGTs at optimal pH (e.g., Noguchi et al, 2007).Vv GT6 catalyzed glucosyl transfer from UDP-Glc to flavonols. Remarkably, this enzyme also displayed a strong galactosyl transfer activity (126% of glucosyl transfer activity) from UDP-Gal to flavonols (Figure 2).…”

mentioning

confidence: 85%

“…Each of these Vv GT genes was predicted to have a single intron. Phylogenetic analysis revealed that each of these genes is related to the GT1 family phylogenetic cluster (cluster I) of flavonoid 3-O-glycosyltransferases, as expected (Vogt and Jones, 2000;Sawada et al, 2005;Noguchi et al, 2007). Moreover, these genes formed a subcluster that was distinct from the Vv GT1-related subcluster ( Figure 1B).…”

Section: Screening Of V Vinifera Flavonoid-3-o-glycosyltransferase Gmentioning

confidence: 96%

“…The branches shown in red and black indicate the foreground and background lineages, respectively, of the UGT gene clusters on the basis of a branch-specific model with the dN/dS ratios of v 1 = 0.34 and v 0 = 0.22, as suggested by the maximum likelihood analysis (Yang, 2007 (Vogt and Jones, 2000) and a catalytic mechanism that inverts the anomeric configuration of a transferred sugar (Campbell et al, 1997;Wang, 2009). Phylogenetic analyses of plant family 1 UGTs show several phylogenetic clusters, which appear to be characterized by the regiospecificity of their glycosyl transfer to flavonoids (Vogt and Jones, 2000;Sawada et al, 2005;Noguchi et al, 2007). Moreover, the differentiation of the sugar donor specificity of UGTs appears to have occurred in a lineage-specific manner after establishment of general regiospecificity for the glycosyl acceptor (Yonekura-Sakakibara et al, 2007;Noguchi et al, 2009a;Ono et al, 2010).…”

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confidence: 99%

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Functional Differentiation of the Glycosyltransferases That Contribute to the Chemical Diversity of Bioactive Flavonol Glycosides in Grapevines (Vitis vinifera)

et al. 2010

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We identified two glycosyltransferases that contribute to the structural diversification of flavonol glycosides in grapevine (Vitis vinifera): glycosyltransferase 5 (Vv GT5) and Vv GT6. Biochemical analyses showed that Vv GT5 is a UDP-glucuronic acid:flavonol-3-O-glucuronosyltransferase (GAT), and Vv GT6 is a bifunctional UDP-glucose/UDP-galactose:flavonol-3-Oglucosyltransferase/galactosyltransferase. The Vv GT5 and Vv GT6 genes have very high sequence similarity (91%) and are located in tandem on chromosome 11, suggesting that one of these genes arose from the other by gene duplication. Both of these enzymes were expressed in accordance with flavonol synthase gene expression and flavonoid distribution patterns in this plant, corroborating their significance in flavonol glycoside biosynthesis. The determinant of the specificity of Vv GT5 for UDP-glucuronic acid was found to be Arg-140, which corresponded to none of the determinants previously identified for other plant GATs in primary structures, providing another example of convergent evolution of plant GAT. We also analyzed the determinants of the sugar donor specificity of Vv GT6. Gln-373 and Pro-19 were found to play important roles in the bifunctional specificity of the enzyme. The results presented here suggest that the sugar donor specificities of these Vv GTs could be determined by a limited number of amino acid substitutions in the primary structures of protein duplicates, illustrating the plasticity of plant glycosyltransferases in acquiring new sugar donor specificities. INTRODUCTIONGrapevine (Vitis vinifera) ( Figure 1A) has been one of the most important fruit crops from the beginning of human civilization (McGovern et al., 1997). Dietary intake of grapevine-based products results in diverse biological effects that are beneficial to human health, in part due to polyphenols, such as flavonoids (e.g., flavonols, proanthocyanidins, and anthocyanins) (Renaud and de Lorgeril, 1992;Corder et al., 2001Corder et al., , 2006Baur et al., 2006). Flavonols, such as kaempferol, quercetin, and isorhamnetin, are an important class of bioactive flavonoids, which are most abundant as their 3-O-glycosides (i.e., glucoside, glucuronoside, galactoside, and rutinoside) in the berries, seeds, and leaves of grapevine (Hmamouchi et al., 1996;Castillo-Munoz et al., 2009).In this plant, biosynthesis of flavonol glycosides primarily serves to protect the plant from excess UV light (Price et al., 1995;Matus et al., 2009). Flavonol aglycons are biosynthesized from dihydroflavonols by the action of flavonol synthase (Vv FLS), a 2-oxoglutarate-dependent dioxygenase, which is temporally regulated by an R2R3-Myb transcription factor, Vv MYBF1 (Fujita et al., 2006;Czemmel et al., 2009). Subsequently, glycosylation of flavonols enhances their water solubility, such that high concentrations of flavonols can accumulate in plant cells.From a food chemistry perspective, flavonol glycosides define the color of wine grapes and products by acting as copigments (Yoshitama et al., 1992;Boulto...

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Section: Biochemical Characterization Of Vv Gt5 and Vv Gt6mentioning

confidence: 54%

Section: Biochemical Characterization Of Vv Gt5 and Vv Gt6mentioning

confidence: 87%

mentioning

confidence: 85%

Section: Screening Of V Vinifera Flavonoid-3-o-glycosyltransferase Gmentioning

confidence: 96%

mentioning

confidence: 99%

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Functional Differentiation of the Glycosyltransferases That Contribute to the Chemical Diversity of Bioactive Flavonol Glycosides in Grapevines (Vitis vinifera)

et al. 2010

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Flavonoid Chemistry of the Leguminosae

Veitch

2010

Recent Advances in Polyphenol Research

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Regio‐ and Stereospecific O‐Glycosylation of Phenolic Compounds Catalyzed by a Fungal Glycosyltransferase from Mucor hiemalis

et al. 2017

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Glycosylated small molecules are often bioactive and obtained mainly via microbial biotransformation especially by fungi. However, no responsible glycosylation gene/enzyme has yet been uncovered in a filamentous fungus. We report here the first identification of a phenolic glycosyltransferase MhGT1 from Mucor hiemalis. The substrate promiscuity of the new phenolic O‐glycosyltransferase was explored by using phenols from Traditional Chinese Medicinal herbs as substrates. MhGT1 exhibited robust capabilities for the regio‐ and stereospecific O‐glycosylation of 72 structurally diverse drug‐like scaffolds and sterols with uridine diphosphate (UDP) glucose as a sugar donor. Unprecedentedly, MhGT1 showed higher regiospecificities and activities for prenylated phenols than for their non‐prenylated analogues. Computational modelling of MhGT1 uncovered a truncated N‐terminal domain of the enzyme consisting of hydrophobic and charged amino acid residues which contributed to the broad substrate scope and regiospecificity towards prenylated compounds. Our findings expand the ways to obtain new glycosyltransferases and also effectively apply the enzymatic approach to obtain glycosylated compounds in drug discovery.magnified image

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A UDP-Glucose:Isoflavone 7-O-Glucosyltransferase from the Roots of Soybean (Glycine max) Seedlings

Cited by 122 publications

References 38 publications

Functional Differentiation of the Glycosyltransferases That Contribute to the Chemical Diversity of Bioactive Flavonol Glycosides in Grapevines (Vitis vinifera)

Functional Differentiation of the Glycosyltransferases That Contribute to the Chemical Diversity of Bioactive Flavonol Glycosides in Grapevines (Vitis vinifera)

Flavonoid Chemistry of the Leguminosae

Regio‐ and Stereospecific O‐Glycosylation of Phenolic Compounds Catalyzed by a Fungal Glycosyltransferase from Mucor hiemalis

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