Evidence map›Paper›PMID 41589901›Full record

ArticlemSystems2026

Catabolism of acetosyringone and co-metabolic transformation of 2,4,6-trichlorophenol by a novel FAD-dependent monooxygenase.

Tomas Engl, Lydie Jakubova, Zdena Skrob, Stephanie Campeggi, Roman Skala, Magdalena Folkmanova, Petr Pajer, Martin Chmel, Tomas Cajthaml, Michal Strejcek and 2 more

Abstract read
In one paragraph

Article in mSystems, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

12 authors.

Tomas EnglDepartment of Biochemistry and Microbiology, Faculty of Food and Biochemical Technology, University of Chemistry and Technology, Prague, Czech Republic.ORCID 0009-0005-1594-3102
Lydie JakubovaDepartment of Biochemistry and Microbiology, Faculty of Food and Biochemical Technology, University of Chemistry and Technology, Prague, Czech Republic.ORCID 0009-0006-6361-831X
Zdena SkrobInstitute of Microbiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic.ORCID 0000-0002-4140-1332
Stephanie CampeggiDepartment of Biochemistry and Microbiology, Faculty of Food and Biochemical Technology, University of Chemistry and Technology, Prague, Czech Republic.ORCID 0009-0006-6278-6952
Roman SkalaDepartment of Biochemistry and Microbiology, Faculty of Food and Biochemical Technology, University of Chemistry and Technology, Prague, Czech Republic.ORCID 0000-0002-0549-6709
Magdalena FolkmanovaDepartment of Biochemistry and Microbiology, Faculty of Food and Biochemical Technology, University of Chemistry and Technology, Prague, Czech Republic.ORCID 0000-0002-6106-5137
Petr PajerMilitary Health Institute, Military Medical Agency, Prague, Czech Republic.ORCID 0000-0002-8706-9371
Martin ChmelMilitary Health Institute, Military Medical Agency, Prague, Czech Republic.ORCID 0000-0003-0864-0574
Tomas CajthamlInstitute of Microbiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic.ORCID 0000-0002-3393-1333
Michal StrejcekDepartment of Biochemistry and Microbiology, Faculty of Food and Biochemical Technology, University of Chemistry and Technology, Prague, Czech Republic.ORCID 0000-0002-6755-5356
Jachym SumanDepartment of Biochemistry and Microbiology, Faculty of Food and Biochemical Technology, University of Chemistry and Technology, Prague, Czech Republic.ORCID 0000-0003-1828-8391
Ondrej UhlikDepartment of Biochemistry and Microbiology, Faculty of Food and Biochemical Technology, University of Chemistry and Technology, Prague, Czech Republic.ORCID 0000-0002-0506-202X

Funding

Grantová Agentura České Republiky 22-00132SMinisterstvo Školství, Mládeže a Tělovýchovy CZ.02.01.01/00/22_008/0004597
6 · The paper itself

Abstract

Acetosyringone (AS), a prototypical syringyl-type monomer of lignin, functions as a model compound for the study of microbial catabolism of S-lignin-derived aromatics. In this study, we present the discovery of a novel metabolic pathway for AS catabolism, initiated by a previously uncharacterized FAD-dependent oxidoreductase, designated AsdA. In contrast to the sole previously documented AS funneling route, which entails side chain modification and conversion to syringic acid, AsdA catalyzes direct hydroxylation of the aromatic core. This represents a mechanistically distinct entry into central metabolism. The identification of this enzyme was achieved through metagenomic and functional analyses of a bacterial consortium enriched on AS as the sole carbon source. The consortium, predominantly comprising

Indexed as

Bacterial ProteinsChlorophenolsFlavin-Adenine DinucleotideMixed Function OxygenasesAcetophenonesMetabolic Networks and PathwaysPseudomonas2,4,6-trichlorophenolAcetophenonesacetosyringoneBacterial ProteinsChlorophenolsFlavin-Adenine DinucleotideMixed Function Oxygenases2,4,6-trichlorophenol (2,4,6-TCP)acetosyringone (AS)aromatic pollutants (APs)chlorophenols (CPs)co-metabolismdegradationFAD-dependent monooxygenase AsdAmetagenome-assembled genomes (MAGs)secondary plant metabolites (SPMs)

Identifiers

PMID41589901
PMCPMC12911418

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.