Evidence map›Paper›PMID 34796596›Full record

ArticleAngewandte Chemie (International ed. in English)2022

Structural Insight into the Catalytic Mechanism of the Endoperoxide Synthase FtmOx1.

Lian Wu, Zhanfeng Wang, Yixin Cen, Binju Wang, Jiahai Zhou

Abstract read
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In one paragraph

Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

12 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Enzymatic Peroxidation in the Chemoenzymatic Synthesis of 13-Oxoverruculogen.Synlett : accounts and rapid communications in synthetic organic chemistry · 2025
    Article
  5. Article
  6. Article
  7. Chemoenzymatic Synthesis of 13-Oxoverruculogen.Journal of the American Chemical Society · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Structural basis for endoperoxide-forming oxygenases.Beilstein journal of organic chemistry · 2022
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Lian WuThe Research Center of Chiral Drugs, Innovation Research Institute of Traditional Chinese Medicine (IRI), Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, China.ORCID 0000-0003-3110-7380
Zhanfeng WangState Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Chemistry and Chemical Engineering, Xiamen University, Xiamen, 361005, China.
Yixin CenThe Research Center of Chiral Drugs, Innovation Research Institute of Traditional Chinese Medicine (IRI), Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, China.ORCID 0000-0002-5851-3170
Binju WangState Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Chemistry and Chemical Engineering, Xiamen University, Xiamen, 361005, China.ORCID 0000-0002-3353-9411
Jiahai ZhouCAS Key Laboratory of Quantitative Engineering Biology, Shenzhen Institute of Synthetic Biology, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen, 518055, China.ORCID 0000-0001-5795-3804
Shanghai University of Traditional Chinese Medicine · CNXiamen University · CNChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 2-oxoglutarate (2OG)-dependent non-heme enzyme FtmOx1 catalyzes the endoperoxide biosynthesis of verruculogen. Although several mechanistic studies have been carried out, the catalytic mechanism of FtmOx1 is not well determined owing to the lack of a reliable complex structure of FtmOx1 with fumitremorgin B. Herein we provide the X-ray crystal structure of the ternary complex FtmOx1⋅2OG⋅fumitremorgin B at a resolution of 1.22 Å. Our structures show that the binding of fumitremorgin B induces significant compression of the active pocket and that Y68 is in close proximity to C26 of the substrate. Further MD simulation and QM/MM calculations support a CarC-like mechanism, in which Y68 acts as the H atom donor for quenching the C26-centered substrate radical. Our results are consistent with all available experimental data and highlight the importance of accurate complex structures in the mechanistic study of enzymatic catalysis.

Indexed as

DioxygenasesCatalysisFungal ProteinsKetoglutaric AcidsQuantum TheoryDioxygenasesfumitremorgin B endoperoxidaseFungal ProteinsKetoglutaric Acidsbiosynthesisendoperoxidesnon-heme enzymesquantum mechanics/molecular mechanicsstructural biology

Identifiers

PMID34796596
OpenAlexW3211449772

What OpenQuestion holds

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Read underepoch 390

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.