Evidence map›Paper›PMID 28114276›Full record

ArticleNature chemical biology2017

Enzyme-catalyzed cationic epoxide rearrangements in quinolone alkaloid biosynthesis.

Yi Zou, Marc Garcia-Borràs, Mancheng C Tang, Yuichiro Hirayama, Dehai H Li, Li Li, Kenji Watanabe, K N Houk, Yi Tang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

23 citing papers in PubMed, 57 citations in OpenAlex.

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  17. On the current role of hydratases in biocatalysis.Applied microbiology and biotechnology · 2018
    Review
  18. Article
  19. Review
  20. Asymmetric Alkene and Arene Halofunctionalization Reactions in Meroterpenoid Biosynthesis.Synlett : accounts and rapid communications in synthetic organic chemistry · 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

9 authors at 3 institutions in 3 countries.

Yi ZouDepartment of Chemical and Biomolecular Engineering, University of California, Los Angeles, Los Angeles, California, USA.
Marc Garcia-BorràsDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California, USA.ORCID 0000-0001-9458-1114
Mancheng C TangDepartment of Chemical and Biomolecular Engineering, University of California, Los Angeles, Los Angeles, California, USA.
Yuichiro HirayamaDepartment of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, Japan.
Dehai H LiKey Laboratory of Marine Drugs, Chinese Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, Qingdao, China.
Li LiDepartment of Chemical and Biomolecular Engineering, University of California, Los Angeles, Los Angeles, California, USA.
Kenji WatanabeDepartment of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, Japan.
K N HoukDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California, USA.
Yi TangDepartment of Chemical and Biomolecular Engineering, University of California, Los Angeles, Los Angeles, California, USA.
University of California, Los Angeles · USUniversity of Shizuoka · JPOcean University of China · CN

Funding

MIRA: Enzymology and Self-Resistance of Natural Product BiosynthesisR35GM118056 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Yi Tang · 2016 to 2026
$6.1M
Rediscovering Natural Chemical Diversity -1DP1GM106413DP1GM106413 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TANG, YI · 2012 to 2016
$3.9M
NIGMS NIH HHS DP1 GM106413NIGMS NIH HHS R35 GM118056
6 · The paper itself

Abstract

Epoxides are highly useful synthons and biosynthons for the construction of complex natural products during total synthesis and biosynthesis, respectively. Among enzyme-catalyzed epoxide transformations, a reaction that is notably missing, in regard to the synthetic toolbox, is cationic rearrangement that takes place under strong acid. This is a challenging transformation for enzyme catalysis, as stabilization of the carbocation intermediate upon epoxide cleavage is required. Here, we discovered two Brønsted acid enzymes that can catalyze two unprecedented epoxide transformations in biology. PenF from the penigequinolone pathway catalyzes a cationic epoxide rearrangement under physiological conditions to generate a quaternary carbon center, while AsqO from the aspoquinolone pathway catalyzes a 3-exo-tet cyclization to forge a cyclopropane-tetrahydrofuran ring system. The discovery of these new epoxide-modifying enzymes further highlights the versatility of epoxides in complexity generation during natural product biosynthesis.

Indexed as

BiocatalysisAlkaloidsAspergillus nidulansCationsEpoxy CompoundsHydro-LyasesMolecular StructurePenicilliumQuantum TheoryQuinolonesAlkaloidsCationsEpoxy CompoundsHydro-LyasesQuinolones

Identifiers

PMID28114276
PMCPMC5310975
OpenAlexW2580466919

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.