Evidence map›Paper›PMID 23258535›Full record

ArticleThe Journal of biological chemistry2013

Glycosyltransferases from oat (Avena) implicated in the acylation of avenacins.

Amorn Owatworakit, Belinda Townsend, Thomas Louveau, Helen Jenner, Martin Rejzek, Richard K Hughes, Gerhard Saalbach, Xiaoquan Qi, Saleha Bakht, Abhijeet Deb Roy and 4 more

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. 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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

22 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Comprehensive mutant chemotyping reveals embedding of a lineage-specific biosynthetic gene cluster in wider plant metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  17. A conserved amino acid residue critical for product and substrate specificity in plant triterpene synthases.Proceedings of the National Academy of Sciences of the United States of America · 2016
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  19. Delivering sustainable crop protection systems via the seed: exploiting natural constitutive and inducible defence pathways.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014
    Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

14 authors at 4 institutions in 1 country.

Amorn OwatworakitDepartment of Metabolic Biology, The John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Belinda Townsend
Thomas Louveau
Helen Jenner
Martin Rejzek
Richard K Hughes
Gerhard Saalbach
Xiaoquan Qi
Saleha Bakht
Abhijeet Deb Roy
Sam T Mugford
Rebecca J M Goss
Robert A Field
Anne Osbourn
Norwich Research Park · GBJohn Innes Centre · GBUniversity of East Anglia · GBSainsbury Laboratory · GB

Funding

Biotechnology and Biological Sciences Research Council 83/P13269Biotechnology and Biological Sciences Research Council BB/C504435/1Biotechnology and Biological Sciences Research Council BB/E009913/1Biotechnology and Biological Sciences Research Council BBS/E/J/00000614Biotechnology and Biological Sciences Research Council BBS/E/J/000C0618
6 · The paper itself

Abstract

Plants produce a huge array of specialized metabolites that have important functions in defense against biotic and abiotic stresses. Many of these compounds are glycosylated by family 1 glycosyltransferases (GTs). Oats (Avena spp.) make root-derived antimicrobial triterpenes (avenacins) that provide protection against soil-borne diseases. The ability to synthesize avenacins has evolved since the divergence of oats from other cereals and grasses. The major avenacin, A-1, is acylated with N-methylanthranilic acid. Previously, we have cloned and characterized three genes for avenacin synthesis (for the triterpene synthase SAD1, a triterpene-modifying cytochrome P450 SAD2, and the serine carboxypeptidase-like acyl transferase SAD7), which form part of a biosynthetic gene cluster. Here, we identify a fourth member of this gene cluster encoding a GT belonging to clade L of family 1 (UGT74H5), and show that this enzyme is an N-methylanthranilic acid O-glucosyltransferase implicated in the synthesis of avenacin A-1. Two other closely related family 1 GTs (UGT74H6 and UGT74H7) are also expressed in oat roots. One of these (UGT74H6) is able to glucosylate both N-methylanthranilic acid and benzoic acid, whereas the function of the other (UGT74H7) remains unknown. Our investigations indicate that UGT74H5 is likely to be key for the generation of the activated acyl donor used by SAD7 in the synthesis of the major avenacin, A-1, whereas UGT74H6 may contribute to the synthesis of other forms of avenacin that are acylated with benzoic acid.

Indexed as

AcylationAvenaCytochrome P-450 Enzyme SystemGene Expression Regulation, EnzymologicGene Expression Regulation, PlantGlycosyltransferasesMultigene FamilyPlant ProteinsPlant RootsSaponinsavenacin A 1Cytochrome P-450 Enzyme SystemGlycosyltransferasesPlant ProteinsSaponins

Identifiers

PMID23258535
PMCPMC3567625
OpenAlexW1998028743

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.