Evidence map›Paper›PMID 38772214›Full record

ReviewCurrent opinion in chemical biology2024

Multinuclear non-heme iron dependent oxidative enzymes (MNIOs) involved in unusual peptide modifications.

Jeff Y Chen, Wilfred A van der Donk

Abstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Thiooxazole Formation on a NontypeablebioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Co-opting the bacterial lipoprotein pathway for the biosynthesis of lipidated macrocyclic peptides.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. RadicalJournal of the American Chemical Society · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. ThiF-Like Enzyme Chemistry in Primary and Secondary Metabolism.Chembiochem : a European journal of chemical biology · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Indolylamide Macrocyclization by aOrganic letters · 2025
    Article
  20. Heme Oxygenase-Like Metalloenzymes.Annual review of biochemistry · 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

2 authors.

Jeff Y ChenDepartment of Chemistry, The Carl R. Woese Institute for Genomic Biology, The Howard Hughes Medical Institute at the University of Illinois at Urbana-Champaign, 1206 W Gregory Drive, Urbana, IL 61801, USA.
Wilfred A van der DonkDepartment of Chemistry, The Carl R. Woese Institute for Genomic Biology, The Howard Hughes Medical Institute at the University of Illinois at Urbana-Champaign, 1206 W Gregory Drive, Urbana, IL 61801, USA. Electronic address: vddonk@illinois.edu.

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
NIGMS NIH HHS R37 GM058822
6 · The paper itself

Abstract

Multinuclear non-heme iron dependent oxidative enzymes (MNIOs), formerly known as domain of unknown function 692 (DUF692), are involved in the post-translational modification of peptides during the biosynthesis of peptide-based natural products. These enzymes catalyze highly unusual and diverse chemical modifications. Several class-defining features of this large family (>14 000 members) are beginning to emerge. Structurally, the enzymes are characterized by a TIM-barrel fold and a set of conserved residues for a di- or tri-iron binding site. They use molecular oxygen to modify peptide substrates, often in a four-electron oxidation taking place at a cysteine residue. This review summarizes the current understanding of MNIOs. Four modifications are discussed in detail: oxazolone-thioamide formation, β-carbon excision, hydantoin-macrocycle formation, and 5-thiooxazole formation. Briefly discussed are two other reactions that do not take place on Cys residues.

Indexed as

Oxidation-ReductionPeptidesProtein Processing, Post-TranslationalHumansIronNonheme Iron ProteinsThioamidesIronNonheme Iron ProteinsPeptidesThioamidesDinuclear/trinuclear iron enzymeMetalloenzymeMetallophoreNatural product biosynthesisRiPPs

Identifiers

PMID38772214
PMCPMC11806912

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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.