Evidence map›Paper›PMID 26456915›Full record

ArticleNature communications2015

The thiostrepton A tryptophan methyltransferase TsrM catalyses a cob(II)alamin-dependent methyl transfer reaction.

Alhosna Benjdia, Stéphane Pierre, Carmen Gherasim, Alain Guillot, Manon Carmona, Patricia Amara, Ruma Banerjee, Olivier Berteau

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Biosynthesis of the Biphenomycin Family of Potent Antibiotics.Angewandte Chemie (International ed. in English) · 2025
    Article
  6. Structural Evidence for DUF512 as a RadicalACS bio & med chem Au · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Functional Diversity of HemN-like Proteins.ACS bio & med chem Au · 2022
    Review
  12. The Atypical Cobalamin-DependentJournal of the American Chemical Society · 2022
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Methanogenesis marker protein 10 (Mmp10) fromThe Journal of biological chemistry · 2019
    Article
  20. Biosynthesis of the Thiopeptins and Identification of an FJournal of the American Chemical Society · 2018
    Article
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 3 institutions in 2 countries.

Alhosna BenjdiaINRA, ChemSyBio, UMR 1319 Micalis, F-78350 Jouy-en-Josas, France.
Stéphane PierreINRA, ChemSyBio, UMR 1319 Micalis, F-78350 Jouy-en-Josas, France.
Carmen GherasimDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109-0600, USA.
Alain GuillotINRA, ChemSyBio, UMR 1319 Micalis, F-78350 Jouy-en-Josas, France.
Manon CarmonaINRA, ChemSyBio, UMR 1319 Micalis, F-78350 Jouy-en-Josas, France.
Patricia AmaraMetalloproteins Unit, Institut de Biologie Structurale, UMR5075, CEA, CNRS, Univ. Grenoble-Alpes. 71, Avenue des Martyrs, CS 10090, 38044 Grenoble, France.
Ruma BanerjeeDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109-0600, USA.
Olivier BerteauINRA, ChemSyBio, UMR 1319 Micalis, F-78350 Jouy-en-Josas, France.
AgroParisTech · FRUniversity of Michigan · USCentre National de la Recherche Scientifique · FR

Funding

REACTION MECHANISMS OF MAMMALIAN B12-DEPENDENT ENZYMESR01DK045776 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI RUMA V BANERJEE · 1998 to 2026
$9.7M
European Research Council 617053NIDDK NIH HHS R01 DK045776
6 · The paper itself

Abstract

Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a novel class of natural products including several antibiotics and bacterial toxins. In countless RiPP biosynthetic pathways, cobalamin-dependent radical SAM (B12/rSAM) enzymes play a pivotal role. In the biosynthetic pathway of the antibiotic and anti-cancer agent thiostrepton A, TsrM, a B12/rSAM enzyme, catalyses the transfer of a methyl group to an electrophilic carbon atom of tryptophan. Here we show that methylcob(III)alamin is the probable physiological enzyme cofactor, and cob(II)alamin rather than cob(I)alamin is a key reaction intermediate. Furthermore, we establish that TsrM and a triple-alanine mutant alkylate cob(II)alamin efficiently leading to the synthesis of MeCbl. Exploiting TsrM substrate ambiguity, we demonstrate that TsrM does not catalyse substrate H-atom abstraction like most radical SAM enzymes. Based on these data, we propose an unprecedented radical-based C-methylation mechanism, which further expands the chemical versatility of rSAM enzymes.

Indexed as

CoenzymesEscherichia coliMethyltransferasesThiostreptonTryptophanVitamin B 12cob(II)alaminCoenzymesmecobalaminMethyltransferasesThiostreptonTryptophanVitamin B 12

Identifiers

PMID26456915
PMCPMC4632189
OpenAlexW2408992521

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.