Evidence map›Paper›PMID 41048116›Full record

ReviewChembiochem : a European journal of chemical biology2025

ThiF-Like Enzyme Chemistry in Primary and Secondary Metabolism.

Keelie S Butler, Anshul Rajput, Jonathan R Chekan

Abstract readReview
In one paragraph

Review in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Late-Stage Posttranslational Assembly of Fosfazinomycins.bioRxiv : the preprint server for biology · 2026
    Article
  2. ThiF-Like Enzyme Chemistry in Primary and Secondary Metabolism.Chembiochem : a European journal of chemical biology · 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

3 authors.

Keelie S ButlerDepartment of Chemistry and Biochemistry, University of North Carolina at Greensboro, Greensboro, NC, 27402, USA.ORCID https://orcid.org/0000-0002-5528-9222
Anshul RajputDepartment of Chemistry and Biochemistry, University of North Carolina at Greensboro, Greensboro, NC, 27402, USA.ORCID https://orcid.org/0000-0002-7777-9804
Jonathan R ChekanDepartment of Chemistry and Biochemistry, University of North Carolina at Greensboro, Greensboro, NC, 27402, USA.ORCID https://orcid.org/0000-0003-4651-0594

Funding

Bioinformatic Guided Discovery and Characterization of New RiPP Natural ProductsR35GM147439 · NIGMS · UNIVERSITY OF NORTH CAROLINA GREENSBORO · PI Jonathan Rodi Chekan · 2022 to 2026
$1.8M
Predoctoral Training: Innovative Technologies for Natural Products and Integrative Medicine ResearchT32AT008938 · NCCIH · UNIVERSITY OF NORTH CAROLINA GREENSBORO · PI Nadja B Cech, Jonathan Rodi Chekan · 2016 to 2026
$1.6M
NCCIH NIH HHS T32 AT008938NCCIH NIH HHS T32AT008938NIGMS NIH HHS R35 GM147439NIH HHS R35GM147439
6 · The paper itself

Abstract

ThiF-like proteins are members of the widespread E1-like enzyme superfamily. The eponymous ThiF enzyme was first described in thiamin biosynthesis as part of Escherichia coli's primary metabolism, and homologous proteins have been subsequently discovered in secondary metabolism. These ThiF-like enzymes are united in their defining ability to perform nucleotidylation of a carboxyl group to generate an activated, electrophilic intermediate, a feature it shares with the structurally related ubiquitin-activating enzymes. From here, an array of different nucleophiles are used across distinct biosynthetic pathways to yield diverse structural scaffolds. In this review, we discuss various ThiF-like enzymes that perform nucleotidylation to facilitate a diverse array of interesting and rare chemistry on different types of substrates, as well as showcase some of the shared structural features.

Indexed as

Escherichia coli ProteinsUbiquitin-Activating EnzymesEscherichia coliSecondary MetabolismThiamineEscherichia coli ProteinsThiamineUbiquitin-Activating Enzymesbiosynthesisnatural productspeptide modificationsRiPPsThiF‐like enzymes

Identifiers

PMID41048116
PMCPMC12596934

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.