Evidence map›Paper›PMID 28103392›Full record

ArticleChembiochem : a European journal of chemical biology2017

A Peroxygenase from Chaetomium globosum Catalyzes the Selective Oxygenation of Testosterone.

Jan Kiebist, Kai-Uwe Schmidtke, Jörg Zimmermann, Harald Kellner, Nico Jehmlich, René Ullrich, Daniel Zänder, Martin Hofrichter, Katrin Scheibner

Open access · bronzeAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed, 80 citations in OpenAlex.

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  6. Rapid screening system to identify unspecific peroxygenase activity.Clinical hemorheology and microcirculation · 2025
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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

9 authors at 4 institutions in 1 country.

Jan KiebistFaculty of Environment and Natural Sciences, Brandenburg University of Technology Cottbus-Senftenberg, Universitätsplatz 1, 01968, Senftenberg, Germany.
Kai-Uwe SchmidtkeFaculty of Environment and Natural Sciences, Brandenburg University of Technology Cottbus-Senftenberg, Universitätsplatz 1, 01968, Senftenberg, Germany.
Jörg ZimmermannFaculty of Environment and Natural Sciences, Brandenburg University of Technology Cottbus-Senftenberg, Universitätsplatz 1, 01968, Senftenberg, Germany.
Harald KellnerDepartment of Bio- and Environmental Sciences, TU Dresden, International Institute Zittau, Markt 23, 02763, Zittau, Germany.
Nico JehmlichDepartment of Molecular Systems Biology, Helmholtz-Centre for Environmental Research, UFZ, Permoserstrasse 15, 04318, Leipzig, Germany.
René UllrichDepartment of Bio- and Environmental Sciences, TU Dresden, International Institute Zittau, Markt 23, 02763, Zittau, Germany.
Daniel ZänderJenaBios GmbH, Löbstedter Strasse 80, 07749, Jena, Germany.
Martin HofrichterDepartment of Bio- and Environmental Sciences, TU Dresden, International Institute Zittau, Markt 23, 02763, Zittau, Germany.
Katrin ScheibnerFaculty of Environment and Natural Sciences, Brandenburg University of Technology Cottbus-Senftenberg, Universitätsplatz 1, 01968, Senftenberg, Germany.
Brandenburg University of Technology Cottbus-Senftenberg · DEInternational University Institute · DEHelmholtz Centre for Environmental Research · DEJena Bioscience (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Unspecific peroxygenases (UPO, EC 1.11.2.1) secreted by fungi open an efficient way to selectively oxyfunctionalize diverse organic substrates, including less-activated hydrocarbons, by transferring peroxide-borne oxygen. We investigated a cell-free approach to incorporate epoxy and hydroxyl functionalities directly into the bulky molecule testosterone by a novel unspecific peroxygenase (UPO) that is produced by the ascomycetous fungus Chaetomium globosum in a complex medium rich in carbon and nitrogen. Purification by fast protein liquid chromatography revealed two enzyme fractions with the same molecular mass (36 kDa) and with specific activity of 4.4 to 12 U mg

Indexed as

Amino Acid SequenceCatalysisChaetomiumChemistry, PharmaceuticalChromatography, High Pressure LiquidMixed Function OxygenasesOxygenTestosteroneMixed Function OxygenasesOxygenperoxygenaseTestosteroneepoxidationhydroxylationoxyfunctionalizationperoxidasesteroid

Identifiers

PMID28103392
PMCPMC5363369
OpenAlexW2577110751

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.