Evidence map›Paper›PMID 29444327›Full record

ArticlePlant & cell physiology2018

Structural and Functional Analysis of UGT92G6 Suggests an Evolutionary Link Between Mono- and Disaccharide Glycoside-Forming Transferases.

Fong-Chin Huang, Ashok Giri, Melina Daniilidis, Guangxin Sun, Katja Härtl, Thomas Hoffmann, Wilfried Schwab

Erratum issuedAbstract read
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In one paragraph

Article in Plant & cell physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Transcription Profiling of Glycosyltransferases inJournal of agricultural and food chemistry · 2025
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  7. Controllable Iterative β-Glucosylation from UDP-Glucose byJournal of agricultural and food chemistry · 2021
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  11. Micropathogen community identification in ticks (Acari: Ixodidae) using third-generation sequencing.International journal for parasitology. Parasites and wildlife · 2021
    Article
  12. Article
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  17. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Fong-Chin HuangBiotechnology of Natural Products, Technische Universität München, Liesel-Beckmann-Str. 1, D-85354 Freising, Germany.
Ashok GiriBiotechnology of Natural Products, Technische Universität München, Liesel-Beckmann-Str. 1, D-85354 Freising, Germany.
Melina DaniilidisBiotechnology of Natural Products, Technische Universität München, Liesel-Beckmann-Str. 1, D-85354 Freising, Germany.
Guangxin SunBiotechnology of Natural Products, Technische Universität München, Liesel-Beckmann-Str. 1, D-85354 Freising, Germany.
Katja HärtlBiotechnology of Natural Products, Technische Universität München, Liesel-Beckmann-Str. 1, D-85354 Freising, Germany.
Thomas HoffmannBiotechnology of Natural Products, Technische Universität München, Liesel-Beckmann-Str. 1, D-85354 Freising, Germany.
Wilfried SchwabBiotechnology of Natural Products, Technische Universität München, Liesel-Beckmann-Str. 1, D-85354 Freising, Germany.
Technical University of Munich · DENational Chemical Laboratory · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation mediated by UDP-dependent glycosyltransferase (UGT) is one of the most common reactions for the biosynthesis of small molecule glycosides. As glycosides have various biological roles, we characterized UGT genes from grapevine (Vitis vinifera). In silico analysis of VvUGT genes that were highly expressed in leaves identified UGT92G6 which showed sequence similarity to both monosaccharide and disaccharide glucoside-forming transferases. The recombinant UGT92G6 glucosylated phenolics, among them caffeic acid, carvacrol, eugenol and raspberry ketone, and also accepted geranyl glucoside and citronellyl glucoside. Thus, UGT92G6 formed mono- and diglucosides in vitro from distinct compounds. The enzyme specificity constant Vmax/Km ratios indicated that UGT92G6 exhibited the highest specificity towards caffeic acid, producing almost equal amounts of the 3- and 4-O-glucoside. Transient overexpression of UGT92G6 in Nicotiana benthamiana leaves confirmed the production of caffeoyl glucoside; however, the level of geranyl diglucoside was not elevated upon overexpression of UGT92G6, even after co-expression of genes encoding geraniol synthase and geraniol UGT to provide sufficient precursor. Comparative sequence and 3-D structure analysis identified a sequence motif characteristic for monoglucoside-forming UGTs in UGT92G6, suggesting an evolutionary link between mono- and disaccharide glycoside UGTs. Thus, UGT92G6 functions as a mono- and diglucosyltransferase in vitro, but acts as a caffeoyl glucoside UGT in N. benthamiana.

Indexed as

Evolution, MolecularCaffeic AcidsCymenesDisaccharidesEnzyme AssaysGlucosidesGlycosyltransferasesKineticsMetabolomeModels, MolecularMonosaccharidesMonoterpenesPhenolsPhylogenyPlant ExtractsPlant Leavescaffeic acidCaffeic AcidscarvacrolCymenesDisaccharidesgeranyl glucosideGlucosidesGlycosyltransferasesMonosaccharidesMonoterpenesPhenolsPlant ExtractsTerpenes

Identifiers

PMID29444327
OpenAlexW2793712635

What OpenQuestion holds

Textmetadata
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.