Evidence map›Paper›PMID 39838140›Full record

ArticleCommunications chemistry2025

Engineering of acyl ligase domain in non-ribosomal peptide synthetases to change fatty acid moieties of lipopeptides.

Rina Aoki, Eri Kumagawa, Kazuaki Kamata, Hideo Ago, Naoki Sakai, Tomohisa Hasunuma, Naoaki Taoka, Yukari Ohta, Shingo Kobayashi

Abstract read
In one paragraph

Article in Communications chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Dual-functionMicrobiology spectrum · 2026
    Article
  2. Article
  3. Review
  4. Diversity of FAAL enzymes and prediction of their substrate specificity using FAALPred.Protein science : a publication of the Protein Society · 2026
    Article
  5. Review
  6. Review
  7. 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

9 authors.

Rina AokiAgri-Bio Research Center, Kaneka Corporation, Takasago, Hyogo, Japan.ORCID http://orcid.org/0009-0001-0903-5686
Eri KumagawaGunma University Center for Food Science and Wellness, Gunma University, Maebashi, Gunma, Japan.
Kazuaki KamataGunma University Center for Food Science and Wellness, Gunma University, Maebashi, Gunma, Japan.
Hideo AgoRIKEN SPring-8 Center, Sayo-gun, Hyogo, Japan.ORCID http://orcid.org/0000-0002-9040-488X
Naoki SakaiRIKEN SPring-8 Center, Sayo-gun, Hyogo, Japan.
Tomohisa HasunumaGraduate School of Science, Technology, and Innovation, Kobe University, Nada, Kobe, Japan.ORCID http://orcid.org/0000-0002-8382-2362
Naoaki TaokaAgri-Bio Research Center, Kaneka Corporation, Takasago, Hyogo, Japan.
Yukari OhtaGunma University Center for Food Science and Wellness, Gunma University, Maebashi, Gunma, Japan.
Shingo KobayashiAgri-Bio Research Center, Kaneka Corporation, Takasago, Hyogo, Japan. Shingo.Kobayashi@kaneka.co.jp.ORCID http://orcid.org/0009-0001-1286-352X

Funding

New Energy and Industrial Technology Development Organization (NEDO) JPNP20011
6 · The paper itself

Abstract

Cyclic lipopeptides (CLPs) produced by the genus Bacillus are amphiphiles composed of hydrophilic amino acid and hydrophobic fatty acid moieties and are biosynthesised by non-ribosomal peptide synthetases (NRPSs). CLPs are produced as a mixture of homologues with different fatty acid moieties, whose length affects CLP activity. Iturin family lipopeptides are a family of CLPs comprising cyclic heptapeptides and β-amino fatty acids and have antimicrobial activity. There is little research on how the length of the fatty acid moiety of iturin family lipopeptides is determined. Here, we demonstrated that the acyl ligase (AL) domain determines the length of the fatty acid moiety in vivo. In addition, enzyme assays revealed how mutations in the substrate-binding pocket of the AL domain affected substrate specificity in vitro. Our findings have implications for the design of fatty acyl moieties for CLP synthesis using NRPS.

Identifiers

PMID39838140
PMCPMC11751314

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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.