Evidence map›Paper›PMID 35013177›Full record

ArticleNature communications2022

Molecular insights into the unusually promiscuous and catalytically versatile Fe(II)/α-ketoglutarate-dependent oxygenase SptF.

Hui Tao, Takahiro Mori, Heping Chen, Shuang Lyu, Akihito Nonoyama, Shoukou Lee, Ikuro Abe

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

16 citing papers in PubMed, 49 citations in OpenAlex.

  1. Functional Characterization of Two Adjacent Oxygenase Genes,Journal of fungi (Basel, Switzerland) · 2026
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  4. A Substrate-Dependent Bifunctional Dioxygenase fromMolecules (Basel, Switzerland) · 2026
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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

7 authors at 3 institutions in 1 country.

Hui Tao *Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Takahiro Mori *Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan. tmori@mol.f.u-tokyo.ac.jp.ORCID 0000-0002-2754-5858
Heping ChenGraduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Shuang LyuGraduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Akihito NonoyamaSumitomo Dainippon Pharma Co., Ltd, Osaka, Japan.
Shoukou LeeSumitomo Dainippon Pharma Co., Ltd, Osaka, Japan.
Ikuro AbeGraduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan. abei@mol.f.u-tokyo.ac.jp.ORCID 0000-0002-3640-888X
The University of Tokyo · JPSumitomo Dainippon Pharma (Japan) · JPJapan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Non-heme iron and α-ketoglutarate-dependent (Fe/αKG) oxygenases catalyze various oxidative biotransformations. Due to their catalytic flexibility and high efficiency, Fe/αKG oxygenases have attracted keen attention for their application as biocatalysts. Here, we report the biochemical and structural characterizations of the unusually promiscuous and catalytically versatile Fe/αKG oxygenase SptF, involved in the biosynthesis of fungal meroterpenoid emervaridones. The in vitro analysis revealed that SptF catalyzes several continuous oxidation reactions, including hydroxylation, desaturation, epoxidation, and skeletal rearrangement. SptF exhibits extremely broad substrate specificity toward various meroterpenoids, and efficiently produced unique cyclopropane-ring-fused 5/3/5/5/6/6 and 5/3/6/6/6 scaffolds from terretonins. Moreover, SptF also hydroxylates steroids, including androsterone, testosterone, and progesterone, with different regiospecificities. Crystallographic and structure-based mutagenesis studies of SptF revealed the molecular basis of the enzyme reactions, and suggested that the malleability of the loop region contributes to the remarkable substrate promiscuity. SptF exhibits great potential as a promising biocatalyst for oxidation reactions.

Indexed as

AndrosteroneBinding SitesBiocatalysisCations, DivalentCrystallography, X-RayFungal ProteinsGene ExpressionHumansHydroxylationIronKetoglutaric AcidsKineticsModels, MolecularMutationOxidation-ReductionOxidoreductases, N-DemethylatingAndrosteroneCations, DivalentFungal ProteinsIronKetoglutaric AcidsOxidoreductases, N-DemethylatingProgesteroneRecombinant ProteinsTerpenesTestosterone

Identifiers

PMID35013177
PMCPMC8748661
OpenAlexW4226392660

What OpenQuestion holds

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LicenceCC BY
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.