Transcriptome-Wide Identification of an Aurone Glycosyltransferase with Glycosidase Activity from Ornithogalum saundersiae

Yuan, Shuai; Liu, Ming; Yang, Yan; He, Juan; Wang, Yanan; Kong, Jian-Qiang

doi:10.3390/genes9070327

Cited by 6 publications

(4 citation statements)

References 30 publications

(44 reference statements)

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“…Studies reported the identification of a series of UGTs with broad substrate tolerance but also narrow substrate specificity, while transcriptome and metabolome analyses have contributed significantly to the study of glycosylation mechanism in planta. 36 Since generalist UGTs exhibit substrate promiscuity, it is not justified to speak of specificity. In this case, the term substrate tolerance is more appropriate, since specificity refers to a limited number of substrates.…”

Section: Uridine-diphosphate Dependent Glycosyltransferases (Ugt) Fam...mentioning

confidence: 99%

Structure–function relationship of terpenoid glycosyltransferases from plants

et al. 2022

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Section: Uridine-diphosphate Dependent Glycosyltransferases (Ugt) Fam...mentioning

confidence: 99%

Structure–function relationship of terpenoid glycosyltransferases from plants

et al. 2022

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“…The evidence suggests that all three metabolites were monoglucosylated sulfuretins. Coelutions of these metabolites with their standards assigned 1a, 1b and 1c to be sulfuretin 3 -, 4 -and 6-glucoside, respectively [29].…”

Section: Structural Identification Of Sulfuretin Monoglucosidesmentioning

confidence: 98%

“…NMR spectroscopic data were obtained as previously described [29,[34][35][36]. Chemical shifts (d) and coupling constants (J) were provided in ppm and hertz (Hz), respectively.…”

Section: Structural Identificationmentioning

confidence: 99%

OcUGT1-Catalyzed Glucosylation of Sulfuretin Yields Ten Glucosides

et al. 2018

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Sulfuretin glucosides are important sources of innovative drugs. However, few glucosides of sulfuretin have been observed in nature. Therefore, it is urgent to diversify sulfuretin glycosides. Herein, glycosyltransferase (GT)-catalyzed glycodiversification of sulfuretin was achieved. Specifically, a flavonoid GT designated as OcUGT1 was used as a biocatalyst for the glucosylation of sulfuretin with UDP-Glc. The OcUGT1-assisted glucosylation of sulfuretin yielded ten glycosylated products, including three monoglucosides, five diglucosides and two triglucosides. The three monoglucosides were thus identified to be sulfuretin 3′-, 4′- and 6-glucoside according to HR-ESI-TOFMS data and their coelution with respective standards. A major diglucoside was assigned as sulfuretin 4′,6-diglucoside by HR-ESI-TOFMS in conjunction with NMR analysis. The exact structure of the other four diglucosides was not well characterized due to their trace amount. However, they were reasonably inferred as sulfuretin 3′,6-diglucoside, sulfuretin 3′,4′-diglucoside and two disaccharide glucosides. In addition, the structural identification of the remaining two triglucosides was not performed because of their small amount. However, one of the triglucosides was deduced to be sulfuretin 3′,4′,6-triglucoside based on the catalytic behavior of OcUGT1. Of the ten sulfuretin glucosides, at least six were new compounds. This is the first time to obtain monoglucosides, diglucosides and triglucosides of sulfuretin simultaneously by a single glycosyltransferase.

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“…The soluble expressions of OcFLS genes in E. coli were verified by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Next, the bacterially produced OcFLS proteins were purified and quantified as previously described [52,53].…”

Section: Heterologous Expression and Protein Purificationmentioning

confidence: 99%

Characterization of two flavonol synthases with iron-independent flavanone 3-hydroxylase activity from Ornithogalum caudatum Jacq

Sun

Kong

2019

BMC Plant Biol

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Background: Flavonol synthase (FLS) is the key enzyme responsible for the biosynthesis of flavonols, the most abundant flavonoids, which have diverse pharmaceutical effects. Flavonol synthase has been previously found in other species, but not yet in Ornithogalum caudatum. Results: The transcriptome-wide mining and functional characterisation of a flavonol synthase gene family from O. caudatum were reported. Specifically, a small FLS gene family harbouring two members, OcFLS1 and OcFLS2, was isolated from O. caudatum based on transcriptome-wide mining. Phylogenetic analysis suggested that the two proteins showed the closest relationship with FLS proteins. In vitro enzymatic assays indicated OcFLS1 and OcFLS2 were flavonol synthases, catalysing the conversion of dihydroflavonols to flavonols in an iron-dependent fashion. In addition, the two proteins were found to display flavanone 3β-hydroxylase (F3H) activity, hydroxylating flavanones to form dihydroflavonols. Unlike single F3H enzymes, the F3H activity of OcFLS1 and OcFLS2 did not absolutely require iron. However, the presence of sufficient Fe 2+ was demonstrated to be conducive to successive catalysis of flavanones to flavonols. The qRT-PCR analysis demonstrated that both genes were expressed in the leaves, bulbs, and flowers, with particularly high expression in the leaves. Moreover, their expression was regulated by developmental and environmental conditions. Conclusions: OcFLS1 and OcFLS2 from O. caudatum were demonstrated to be flavonol synthases with ironindependent flavanone 3-hydroxylase activity.

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Transcriptome-Wide Identification of an Aurone Glycosyltransferase with Glycosidase Activity from Ornithogalum saundersiae

Cited by 6 publications

References 30 publications

Structure–function relationship of terpenoid glycosyltransferases from plants

Structure–function relationship of terpenoid glycosyltransferases from plants

OcUGT1-Catalyzed Glucosylation of Sulfuretin Yields Ten Glucosides

Characterization of two flavonol synthases with iron-independent flavanone 3-hydroxylase activity from Ornithogalum caudatum Jacq

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