Evidence map›Paper›PMID 25730549›Full record

ArticleNature chemical biology2015

The structure of SpnF, a standalone enzyme that catalyzes [4 + 2] cycloaddition.

Christopher D Fage, Eta A Isiorho, Yungnan Liu, Drew T Wagner, Hung-wen Liu, Adrian T Keatinge-Clay

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

46 citing papers in PubMed, 114 citations in OpenAlex.

  1. The Diels-Alder Reaction as a Key Step in Natural Product Synthesis.Progress in the chemistry of organic natural products · 2026
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  5. Natural product reports · 2023
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  8. Catalysis and Electron Transfer inChemical reviews · 2022
    Review
  9. Article
  10. Article
  11. Homology Modeling,Frontiers in cellular and infection microbiology · 2022
    Article
  12. Article
  13. Article
  14. Review
  15. Enzymatic reactions in teleocidin B biosynthesis.Journal of natural medicines · 2021
    Review
  16. Review
  17. Catalytic mechanism andNature catalysis · 2021
    Article
  18. Article
  19. Review
  20. 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

6 authors at 1 institution in 1 country.

Christopher D FageDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
Eta A IsiorhoDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
Yungnan LiuDivision of Medicinal Chemistry, College of Pharmacy, The University of Texas at Austin, Austin, Texas, USA.
Drew T WagnerDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
Hung-wen Liu1] Division of Medicinal Chemistry, College of Pharmacy, The University of Texas at Austin, Austin, Texas, USA. [2] Department of Chemistry, The University of Texas at Austin, Austin, Texas, USA.
Adrian T Keatinge-Clay1] Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA. [2] Department of Chemistry, The University of Texas at Austin, Austin, Texas, USA.
The University of Texas at Austin · US

Funding

Three-Membered Ring Metabolites, Inhibition &FormationR01GM040541 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LIU, HUNG-WEN · 1989 to 2023
$7.4M
Mechanistic Studies of Deoxy Sugar BiosynthesisR01GM035906 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI LIU, HUNG-WEN · 1986 to 2023
$6.1M
Determining the Architectures and Activities of Polyketide Synthase ModulesR01GM106112 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI KEATINGE-CLAY, ADRIAN TRISTAN · 2013 to 2025
$3.9M
MECHANISMS OF BIOSYNTHETIC FORMATION OF DEOXY SUGARSR37GM035906 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LIU, HUNG-WEN · 1999 to 2008
$3.4M
NIGMS NIH HHS GM035906NIGMS NIH HHS GM040541NIGMS NIH HHS GM106112NIGMS NIH HHS R01 GM035906NIGMS NIH HHS R01 GM040541NIGMS NIH HHS R01 GM106112NIGMS NIH HHS R37 GM035906
6 · The paper itself

Abstract

In the biosynthetic pathway of the spinosyn insecticides, the tailoring enzyme SpnF performs a [4 + 2] cycloaddition on a 22-membered macrolactone to forge an embedded cyclohexene ring. To learn more about this reaction, which could potentially proceed through a Diels-Alder mechanism, we determined the 1.50-Å-resolution crystal structure of SpnF bound to S-adenosylhomocysteine. This sets the stage for advanced experimental and computational studies to determine the precise mechanism of SpnF-mediated cyclization.

Indexed as

Cycloaddition ReactionActinobacteriaCatalysisChaperonin 10Chaperonin 60Chemistry, OrganicCloning, MolecularCrystallography, X-RayCyclizationElectronsEnzymesEscherichia coliInsecticidesIntramolecular LyasesLactonesModels, ChemicalChaperonin 10Chaperonin 60EnzymesInsecticidesIntramolecular LyasesLactones

Identifiers

PMID25730549
PMCPMC4366278
OpenAlexW1985672936

What OpenQuestion holds

Textmetadata
LicenceTDM
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.