Evidence map›Paper›PMID 38745065›Full record

ArticleCommunications biology2024

Structural and mechanistic insights into Quinolone Synthase to address its functional promiscuity.

Mallika Vijayanathan, Abhinav Koyamangalath Vadakkepat, Kozhinjampara R Mahendran, Abdoallah Sharaf, Kristian E H Frandsen, Debashree Bandyopadhyay, M Radhakrishna Pillai, Eppurath Vasudevan Soniya

Abstract read
In one paragraph

Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Unravelling the Functional Diversity of Type III Polyketide Synthases in Fungi.Angewandte Chemie (International ed. in English) · 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

8 authors.

Mallika VijayanathanTransdisciplinary Research Program, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram, 695014, India.ORCID 0000-0001-9806-3736
Abhinav Koyamangalath VadakkepatMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Kozhinjampara R MahendranTransdisciplinary Research Program, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram, 695014, India.ORCID 0000-0003-2549-9250
Abdoallah SharafSequAna Core Facility, Department of Biology, University of Konstanz, Konstanz, Germany.ORCID 0000-0002-3436-9290
Kristian E H FrandsenDepartment of Plant and Environment Sciences, University of Copenhagen, 1871, Frederiksberg C, Denmark.ORCID 0000-0002-7136-9820
Debashree BandyopadhyayDepartment of Biological Sciences, Birla Institute of Technology and Science, Hyderabad, India.
M Radhakrishna PillaiCancer Research Program, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram, 695014, India.
Eppurath Vasudevan SoniyaTransdisciplinary Research Program, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram, 695014, India. evsoniya@rgcb.res.in.ORCID 0000-0003-4248-3891

Funding

Council of Scientific and Industrial Research (CSIR) 09/716(0178)/2018-EMR-1
6 · The paper itself

Abstract

Quinolone synthase from Aegle marmelos (AmQNS) is a type III polyketide synthase that yields therapeutically effective quinolone and acridone compounds. Addressing the structural and molecular underpinnings of AmQNS and its substrate interaction in terms of its high selectivity and specificity can aid in the development of numerous novel compounds. This paper presents a high-resolution AmQNS crystal structure and explains its mechanistic role in synthetic selectivity. Additionally, we provide a model framework to comprehend structural constraints on ketide insertion and postulate that AmQNS's steric and electrostatic selectivity plays a role in its ability to bind to various core substrates, resulting in its synthetic diversity. AmQNS prefers quinolone synthesis and can accommodate large substrates because of its wide active site entrance. However, our research suggests that acridone is exclusively synthesized in the presence of high malonyl-CoA concentrations. Potential implications of functionally relevant residue mutations were also investigated, which will assist in harnessing the benefits of mutations for targeted polyketide production. The pharmaceutical industry stands to gain from these findings as they expand the pool of potential drug candidates, and these methodologies can also be applied to additional promising enzymes.

Indexed as

QuinolonesCatalytic DomainCrystallography, X-RayModels, MolecularPolyketide SynthasesProtein ConformationSubstrate SpecificityPolyketide SynthasesQuinolones

Identifiers

PMID38745065
PMCPMC11093982

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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.