Evidence map›Paper›PMID 29343058›Full record

ArticleJournal of the American Chemical Society2018

Biosynthesis of Long-Chain N-Acyl Amide by a Truncated Polyketide Synthase-Nonribosomal Peptide Synthetase Hybrid Megasynthase in Fungi.

Yang Hai, Yi Tang

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. NewSynthetic and systems biotechnology · 2024
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Transcriptional Activation of Biosynthetic Gene Clusters in Filamentous Fungi.Frontiers in bioengineering and biotechnology · 2022
    Review
  10. Biosynthesis of depsipeptides, or Depsi: The peptides with varied generations.Protein science : a publication of the Protein Society · 2020
    Review
  11. Article
  12. Structure-guided function discovery of an NRPS-like glycine betaine reductase for choline biosynthesis in fungi.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Refining and expanding nonribosomal peptide synthetase function and mechanism.Journal of industrial microbiology & biotechnology · 2019
    Review
  14. Identification of the Pyranonigrin A Biosynthetic Gene Cluster by Genome Mining inAIChE journal. American Institute of Chemical Engineers · 2018
    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

2 authors at 1 institution in 1 country.

Yang HaiDepartment of Chemical and Biomolecular Engineering, ‡Chemistry and Biochemistry, University of California, Los Angeles , Los Angeles, California 90095, United States.ORCID 0000-0002-2039-5367
Yi TangDepartment of Chemical and Biomolecular Engineering, ‡Chemistry and Biochemistry, University of California, Los Angeles , Los Angeles, California 90095, United States.ORCID 0000-0003-1597-0141
University of California, Los Angeles · US

Funding

MIRA: Enzymology and Self-Resistance of Natural Product BiosynthesisR35GM118056 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Yi Tang · 2016 to 2026
$6.1M
NIGMS NIH HHS R35 GM118056
6 · The paper itself

Abstract

Truncated iterative polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) megasynthases in which only the C domain is present are widespread in fungi, yet nearly all members have unknown functions. Bioinformatics analysis showed that the C domains of such PKS-C enzymes are noncanonical due to substitution at the second histidine in the active site HHxxxDG motif. Here, we used genome mining strategy to characterize a cryptic PKS-C hybrid from Talaromyces wortmanii and discovered the products are reduced long-chain polyketides amidated with a specific ω-amino acid 5-aminopentanoic acid (5PA). The wortmanamides resemble long-chain N-acyl-amide signaling lipids that target diverse receptors including GPCRs. The noncanonical C domain of this PKS-C hybrid was also demonstrated to be a bona fide condensation domain that specifically selects 5PA and catalyzes amidation to release polyketide chain.

Indexed as

AmidesMolecular ConformationPeptide SynthasesPolyketide SynthasesTalaromycesAmidesnon-ribosomal peptide synthasePeptide SynthasesPolyketide Synthases

Identifiers

PMID29343058
PMCPMC5817892
OpenAlexW2783533016

What OpenQuestion holds

Textmetadata
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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.