Evidence map›Paper›PMID 29190095›Full record

ArticleJournal of the American Chemical Society2017

Mechanism of a Class C Radical S-Adenosyl-l-methionine Thiazole Methyl Transferase.

Zhengan Zhang, Nilkamal Mahanta, Graham A Hudson, Douglas A Mitchell, Wilfred A van der Donk

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Structural and Spectroscopic Basis for Catalysis by a Class C RadicalJournal of the American Chemical Society · 2026
    Article
  3. Structural and Spectroscopic Basis for Catalysis by a Class C RadicalbioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Enzymatic Pyridine Aromatization during Thiopeptide Biosynthesis.Journal of the American Chemical Society · 2022
    Article
  7. Functional Diversity of HemN-like Proteins.ACS bio & med chem Au · 2022
    Review
  8. Review
  9. HutW fromBiochemistry · 2021
    Article
  10. Review
  11. Article
  12. Review
  13. Methanogenesis marker protein 10 (Mmp10) fromThe Journal of biological chemistry · 2019
    Article
  14. RiPP antibiotics: biosynthesis and engineering potential.Current opinion in microbiology · 2018
    Review
  15. Article
  16. Review
  17. 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

5 authors at 2 institutions in 1 country.

Zhengan ZhangDepartment of Chemistry, University of Illinois at Urbana-Champaign , Urbana, Illinois 61801, United States.
Nilkamal MahantaDepartment of Chemistry, University of Illinois at Urbana-Champaign , Urbana, Illinois 61801, United States.
Graham A HudsonDepartment of Chemistry, University of Illinois at Urbana-Champaign , Urbana, Illinois 61801, United States.
Douglas A MitchellDepartment of Chemistry, University of Illinois at Urbana-Champaign , Urbana, Illinois 61801, United States.ORCID 0000-0002-9564-0953
Wilfred A van der DonkDepartment of Chemistry, University of Illinois at Urbana-Champaign , Urbana, Illinois 61801, United States.ORCID 0000-0002-5467-7071
University of Illinois Urbana-Champaign · USHoward Hughes Medical Institute · US

Funding

Enzyme Chemistry and Biological Function of RiPP-like Modifications.R01GM097142 · NIGMS · VANDERBILT UNIVERSITY · PI MITCHELL, DOUGLAS ALAN · 2012 to 2024
$4.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM097142
6 · The paper itself

Abstract

The past decade has seen the discovery of four different classes of radical S-adenosylmethionine (rSAM) methyltransferases that methylate unactivated carbon centers. Whereas the mechanism of class A is well understood, the molecular details of methylation by classes B-D are not. In this study, we present detailed mechanistic investigations of the class C rSAM methyltransferase TbtI involved in the biosynthesis of the potent thiopeptide antibiotic thiomuracin. TbtI C-methylates a Cys-derived thiazole during posttranslational maturation. Product analysis demonstrates that two SAM molecules are required for methylation and that one SAM (SAM1) is converted to 5'-deoxyadenosine and the second SAM (SAM2) is converted to S-adenosyl-l-homocysteine (SAH). Isotope labeling studies show that a hydrogen is transferred from the methyl group of SAM2 to the 5'-deoxyadenosine of SAM1 and the other two hydrogens of the methyl group of SAM2 appear in the methylated product. In addition, a hydrogen appears to be transferred from the β-position of the thiazole to the methyl group in the product. We also show that the methyl protons in the product can exchange with solvent. A mechanism consistent with these observations is presented that differs from other characterized radical SAM methyltransferases.

Indexed as

Anti-Bacterial AgentsDeoxyadenosinesHydrogenMethylationMethyltransferasesPeptides, CyclicProtonsS-AdenosylhomocysteineS-AdenosylmethionineSolventsThiazoles2'-deoxyadenosineAnti-Bacterial AgentsDeoxyadenosinesHydrogenMethyltransferasesPeptides, CyclicProtonsS-AdenosylhomocysteineS-AdenosylmethionineSolventsThiazolesthiomuracin A

Identifiers

PMID29190095
PMCPMC5748327
OpenAlexW2774642737

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.