Evidence map›Paper›PMID 32719482›Full record

ArticleNature chemistry2020

Acyltransferase that catalyses the condensation of polyketide and peptide moieties of goadvionin hybrid lipopeptides.

Ryosuke Kozakai, Takuto Ono, Shotaro Hoshino, Hidenori Takahashi, Yohei Katsuyama, Yoshinori Sugai, Taro Ozaki, Kazuya Teramoto, Kanae Teramoto, Koichi Tanaka and 3 more

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Article in Nature chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

32 citing papers in PubMed, 56 citations in OpenAlex.

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  5. A Revised Model for Muscarine Biosynthesis Involving Lysine Trimethylation.Angewandte Chemie (International ed. in English) · 2026
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  7. Structure, biosynthesis, and bioactivity of nostolysamides.bioRxiv : the preprint server for biology · 2026
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  18. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 2 institutions in 1 country.

Ryosuke Kozakai *Graduate School of Agricultural and Life Sciences, Department of Biotechnology, The University of Tokyo, Tokyo, Japan.ORCID http://orcid.org/0000-0002-3428-8802
Takuto Ono *Graduate School of Agricultural and Life Sciences, Department of Biotechnology, The University of Tokyo, Tokyo, Japan.
Shotaro HoshinoGraduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Hidenori TakahashiKoichi Tanaka Mass Spectrometry Research Laboratory Shimadzu Corporation, Kyoto, Japan.ORCID http://orcid.org/0000-0001-6887-1724
Yohei KatsuyamaGraduate School of Agricultural and Life Sciences, Department of Biotechnology, The University of Tokyo, Tokyo, Japan.ORCID http://orcid.org/0000-0003-4905-5320
Yoshinori SugaiGraduate School of Agricultural and Life Sciences, Department of Biotechnology, The University of Tokyo, Tokyo, Japan.
Taro OzakiGraduate School of Agricultural and Life Sciences, Department of Biotechnology, The University of Tokyo, Tokyo, Japan.
Kazuya TeramotoGraduate School of Agricultural and Life Sciences, Department of Biotechnology, The University of Tokyo, Tokyo, Japan.
Kanae TeramotoKoichi Tanaka Mass Spectrometry Research Laboratory Shimadzu Corporation, Kyoto, Japan.
Koichi TanakaKoichi Tanaka Mass Spectrometry Research Laboratory Shimadzu Corporation, Kyoto, Japan.
Ikuro AbeGraduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.ORCID http://orcid.org/0000-0002-3640-888X
Shumpei AsamizuGraduate School of Agricultural and Life Sciences, Department of Biotechnology, The University of Tokyo, Tokyo, Japan.ORCID http://orcid.org/0000-0002-7178-5410
Hiroyasu OnakaGraduate School of Agricultural and Life Sciences, Department of Biotechnology, The University of Tokyo, Tokyo, Japan. aonaka@mail.ecc.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0003-4536-1881
The University of Tokyo · JPShimadzu (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fusions of fatty acids and peptides expand the structural diversity of natural products; however, polyketide/ribosomally synthesized and post-translationally modified peptides (PK/RiPPs) hybrid lipopeptides are relatively rare. Here we report a family of PK/RiPPs called goadvionins, which inhibit the growth of Gram-positive bacteria, and an acyltransferase, GdvG, which catalyses the condensation of the PK and RiPP moieties. Goadvionin comprises a trimethylammonio 32-carbon acyl chain and an eight-residue RiPP with an avionin structure. The positions of six hydroxyl groups and one double bond in the very-long acyl chain were determined by radical-induced dissociation tandem mass spectrometry, which collides radical ion species to generate C-C bond cleavage fragments. GdvG belongs to the Gcn5-related N-acetyltransferase superfamily. Unlike conventional acyltransferases, GdvG transfers a very long acyl chain that is tethered to an acyl carrier protein to the N-terminal amino group of the RiPP moiety. gdvG homologues flanked by PK/fatty acid and RiPP biosynthesis genes are widely distributed in microbial species, suggesting that acyltransferase-catalysed condensation of PKs and RiPPs is a general strategy in biosynthesis of similar lipopeptides.

Indexed as

AcyltransferasesBiocatalysisLipopeptidesMultigene FamilyNuclear Magnetic Resonance, BiomolecularPolyketidesProtein Processing, Post-TranslationalStreptomycesTandem Mass SpectrometryAcyltransferasesLipopeptidesPolyketides

Identifiers

PMID32719482
OpenAlexW3044457140

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.