Evidence map›Paper›PMID 39214926›Full record

ReviewJournal of natural medicines2025

Macrocyclizing-thioesterases in bacterial non-ribosomal peptide biosynthesis.

Kenichi Matsuda

Abstract readReview
In one paragraph

Review in Journal of natural medicines, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. A chlorinated diketopiperazine antibiotic targetsAntimicrobial agents and chemotherapy · 2025
    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

1 author.

Kenichi MatsudaFaculty of Pharmaceutical Sciences, Hokkaido University, Kita 12, Nishi 6, Kita-ku, Sapporo, 060-0812, Japan. kematsuda@pharm.hokudai.ac.jp.ORCID http://orcid.org/0000-0002-9269-688X

Funding

Japan Agency for Medical Research and Development JP23gm1610007Japan Science and Technology Agency ACT-X JPMJAX201FJapan Society for the Promotion of Science JP22K15302Japan Society for the Promotion of Science JP23K17410Japan Society for the Promotion of Science JP24K01659
6 · The paper itself

Abstract

Macrocyclization of peptides reduces conformational flexibilities, potentially leading to improved drug-like properties. However, side reactions such as epimerization and oligomerization often pose synthetic challenges. Peptide-cyclizing biocatalysts in the biosynthesis of non-ribosomal peptides (NRPs) have remarkable potentials as chemoenzymatic tools to facilitate more straightforward access to complex macrocycles. This review highlights the biocatalytic potentials of NRP cyclases, especially those of cis-acting thioesterases, the most general cyclizing machinery in NRP biosynthesis. Growing insights into penicillin-binding protein-type thioesterases, a relatively new group of trans-acting thioesterases, are also summarized.

Indexed as

BacteriaPeptidesThiolester HydrolasesCyclizationPeptidesThiolester HydrolasesBiosynthesisChemoenzymatic synthesisMacrocyclizationNon-ribosomal peptideThioesterase

Identifiers

PMID39214926
PMCPMC11735501

What OpenQuestion holds

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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.