Evidence map›Paper›PMID 30204409›Full record

ArticleACS chemical biology2018

Molecular Basis for Autocatalytic Backbone N-Methylation in RiPP Natural Product Biosynthesis.

Chayanid Ongpipattanakul, Satish K Nair

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-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

19 citing papers in PubMed, 37 citations in OpenAlex.

  1. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
    Review
  2. Article
  3. Article
  4. Genome Mining and Biological Engineering of Type III Borosins from Bacteria.International journal of molecular sciences · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. A Permissive AmideACS catalysis · 2023
    Article
  9. Article
  10. Structure and mechanism for iterative amideProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Engineering of a Peptide α-N-Methyltransferase to Methylate Non-Proteinogenic Amino Acids.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021
    Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. 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

2 authors at 1 institution in 1 country.

Chayanid Ongpipattanakul
University of Illinois Urbana-Champaign · US

Funding

Structural /Mechanistic Study of Lantibiotic Biosynthetic Enzymes & AutoimmunityR01GM079038 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI NAIR, SATISH K · 2006 to 2023
$3.7M
4800 Plus MALDI TOF/TOF AnalyzerS10RR027109 · NCRR · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI VAN DER DONK, WILFRED A. · 2010 to 2010
$395k
NCRR NIH HHS S10 RR027109NIGMS NIH HHS R01 GM079038
6 · The paper itself

Abstract

N-methylation of nucleic acids, proteins, and peptides is a chemical modification with significant impact on biological regulation. Despite the simplicity of the structural change, N-methylation can influence diverse functions including epigenetics, protein complex formation, and microtubule stability. While there are limited examples of N-methylation of the α-amino group of bacterial and eukaryotic proteins, there are no examples of catalysts that carry out post-translation methylation of backbone amides in proteins or peptides. Recent studies have identified enzymes that catalyze backbone N-methylation on a peptide substrate, a reaction with little biochemical precedent, in a family of ribosomally synthesized natural products produced in basidiomycetes. Here, we describe the crystal structures of Dendrothele bispora dbOphMA, a methyltransferase that catalyzes multiple N-methylations on the peptide backbone. We further carry out biochemical studies of this catalyst to determine the molecular details that promote this unusual chemical transformation. The structural and biochemical framework described here could facilitate biotechnological applications of catalysts for the rapid production of backbone N-methylated peptides.

Indexed as

AgaricalesAmino Acid SequenceCatalytic DomainFungal ProteinsMethylationMethyltransferasesModels, ChemicalMutationPeptidesProtein BindingProtein Processing, Post-TranslationalS-AdenosylhomocysteineS-AdenosylmethionineSubstrate SpecificityFungal ProteinsMethyltransferasesPeptidesS-AdenosylhomocysteineS-Adenosylmethionine

Identifiers

PMID30204409
PMCPMC6340302
OpenAlexW2891147245

What OpenQuestion holds

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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.