Evidence map›Paper›PMID 29253341›Full record

ArticleJournal of the American Chemical Society2018

Mechanistic Investigations of PoyD, a Radical S-Adenosyl-l-methionine Enzyme Catalyzing Iterative and Directional Epimerizations in Polytheonamide A Biosynthesis.

Aubérie Parent, Alhosna Benjdia, Alain Guillot, Xavier Kubiak, Clémence Balty, Benjamin Lefranc, Jérôme Leprince, Olivier Berteau

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

33 citing papers in PubMed, 67 citations in OpenAlex.

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  7. The radical SAM enzyme EpeE exhibits distinct site reactivity during the biosynthesis of the RiPP natural product epipeptide.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

8 authors at 2 institutions in 1 country.

Aubérie ParentMicalis Institute, ChemSyBio, INRA, AgroParisTech, Université Paris-Saclay , 78350 Jouy-en-Josas, France.
Alhosna BenjdiaMicalis Institute, ChemSyBio, INRA, AgroParisTech, Université Paris-Saclay , 78350 Jouy-en-Josas, France.
Alain GuillotMicalis Institute, ChemSyBio, INRA, AgroParisTech, Université Paris-Saclay , 78350 Jouy-en-Josas, France.
Xavier KubiakMicalis Institute, ChemSyBio, INRA, AgroParisTech, Université Paris-Saclay , 78350 Jouy-en-Josas, France.
Clémence BaltyMicalis Institute, ChemSyBio, INRA, AgroParisTech, Université Paris-Saclay , 78350 Jouy-en-Josas, France.
Benjamin LefrancInserm U1239, PRIMACEN, University of Rouen Normandy , 76000 Rouen, France.
Jérôme LeprinceInserm U1239, PRIMACEN, University of Rouen Normandy , 76000 Rouen, France.
Olivier BerteauMicalis Institute, ChemSyBio, INRA, AgroParisTech, Université Paris-Saclay , 78350 Jouy-en-Josas, France.ORCID 0000-0002-3434-5168
AgroParisTech · FRInserm · FR

Funding

European Research Council 617053
6 · The paper itself

Abstract

Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a growing family of bioactive peptides. Among RiPPs, the bacterial toxin polytheonamide A is characterized by a unique set of post-translational modifications catalyzed by novel radical S-adenosyl-l-methionine (SAM) enzymes. Here we show that the radical SAM enzyme PoyD catalyzes in vitro polytheonamide epimerization in a C-to-N directional manner. By combining mutagenesis experiments with labeling studies and investigating the enzyme substrate promiscuity, we deciphered in detail the mechanism of PoyD. We notably identified a critical cysteine residue as a likely key H atom donor and demonstrated that PoyD belongs to a distinct family of radical SAM peptidyl epimerases. In addition, our study shows that the core peptide directly influences the epimerization pattern allowing for production of peptides with unnatural epimerization patterns.

Identifiers

PMID29253341
PMCPMC5824343
OpenAlexW2777114057

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.