Evidence map›Paper›PMID 40931687›Full record

ArticleChembiochem : a European journal of chemical biology2025

Characterization of the N-Hydroxylating Monooxygenase TheA from Thermocrispum agreste Reveals a Broad Substrate Spectrum.

Artur Maier, Daniel Fast, Dmytro Sakalo, Lindelo Mguni, Dirk Tischler

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

5 authors.

Artur MaierFaculty of Biology and Biotechnology, Microbial Biotechnology, Ruhr University Bochum, Universitätsstrasse 150, Bochum, 44780, Germany.ORCID https://orcid.org/0000-0003-0132-4085
Daniel FastFaculty of Biology and Biotechnology, Microbial Biotechnology, Ruhr University Bochum, Universitätsstrasse 150, Bochum, 44780, Germany.
Dmytro SakaloFaculty of Biology and Biotechnology, Microbial Biotechnology, Ruhr University Bochum, Universitätsstrasse 150, Bochum, 44780, Germany.
Lindelo MguniFaculty of Biology and Biotechnology, Microbial Biotechnology, Ruhr University Bochum, Universitätsstrasse 150, Bochum, 44780, Germany.
Dirk TischlerFaculty of Biology and Biotechnology, Microbial Biotechnology, Ruhr University Bochum, Universitätsstrasse 150, Bochum, 44780, Germany.ORCID https://orcid.org/0000-0002-6288-2403

Funding

European Union's Horizon Europe research and innovation program under the Marie 101073065German Research Council (DFG) 321933041German Research Council (DFG) 536337083
6 · The paper itself

Abstract

The N-hydroxylating monooxygenase (NMO) TheA from Thermocrispum agreste catalyzes the N-hydroxylation step of l-ornithine, which is the first step in the thermochelin siderophore biosynthesis. Characterization of this enzyme revealed a significant thermostability up to 50 °C and activity with the non-native substrate d-ornithine with kinetic parameters (K

Indexed as

Mixed Function OxygenasesHydrogen PeroxideHydroxylationKineticsSubstrate SpecificityHydrogen PeroxideMixed Function Oxygenasesamino acid biotransformationbiocatalysisenzyme cascadeflavoprotein monooxygenaseN‐hydroxylation

Identifiers

PMID40931687
PMCPMC12498188

What Socratic holds

Textmetadata
LicenceCC BY
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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 Socratic graph.