Evidence map›Paper›PMID 39819031›Full record

ArticleOrganic letters2025

Transformation-Guided Genome Mining Provides Access to Brominated Lanthipeptides.

Nirmal Saha, F N U Vidya, Youran Luo, Wilfred A van der Donk, Vinayak Agarwal

Abstract read
In one paragraph

Article in Organic letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Article
  2. Peptide Prenylation Follows Divergent Substrate Engagement Rules.Journal of the American Chemical Society · 2025
    Article
  3. Article
  4. Article
  5. PEARLs of wisdom for ribosome-independent peptide bond synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Substrate recognition by a peptide-aminoacyl-tRNA ligase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Peptide halogenation biochemistry: interfacing pharmaceutical deliverables with chemical innovation.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2025
    Review
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

5 authors.

Nirmal SahaSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, United States.
F N U VidyaSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, United States.
Youran LuoDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.ORCID 0000-0002-8033-2472
Wilfred A van der DonkDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.ORCID 0000-0002-5467-7071
Vinayak AgarwalSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, United States.ORCID 0000-0002-2517-589X

Funding

Posttranslational Modifications during Natural Product BiosynthesisR37GM058822 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI VAN DER DONK, WILFRED A. · 2016 to 2025
$2.9M
Halogenation Biochemistry in Human and Environmental HealthR35GM142882 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI AGARWAL, VINAYAK · 2021 to 2025
$1.9M
NIGMS NIH HHS R35 GM142882NIGMS NIH HHS R37 GM058822
6 · The paper itself

Abstract

Natural product biosynthesis is nature's tinkering ground for developing new enzymes that can achieve chemical transformations that are outside the purview of traditional chemical catalysis. Herein we describe a genome mining approach that leads to the discovery of a halogenase that regioselectively brominates a tryptophan side chain indole for a macrocyclic peptide substrate, enabling downstream chemical arylation by Suzuki-Miyaura coupling. The halogenase was found to prefer a macrocyclic peptide substrate over a linear peptide. The brominase presents a starting point for biocatalytic access to macrocyclic peptides bearing a chemically versatile aryl-bromide reactive handle.

Indexed as

HalogenationBiocatalysisHydrocarbons, BrominatedMolecular StructurePeptidesTryptophanHydrocarbons, BrominatedPeptidesTryptophan

Identifiers

PMID39819031
PMCPMC11791876

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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.