Evidence map›Paper›PMID 27392087›Full record

ArticleThe ISME journal2017

An unusual strategy for the anoxic biodegradation of phthalate.

Christa Ebenau-Jehle, Mario Mergelsberg, Stefanie Fischer, Thomas Brüls, Nico Jehmlich, Martin von Bergen, Matthias Boll

Open access · bronzeAbstract read
In one paragraph

Article in The ISME journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
6.0field-weighted citation impact, top 4% 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

18 citing papers in PubMed, 79 citations in OpenAlex.

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  10. Structure and Mechanism ofACS catalysis · 2021
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  16. Towards the Response Threshold forApplied and environmental microbiology · 2018
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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 2 countries.

Christa Ebenau-JehleUniversity of Freiburg, Institute for Biology II, Freiburg, Germany.
Mario MergelsbergUniversity of Freiburg, Institute for Biology II, Freiburg, Germany.
Stefanie FischerUniversity of Freiburg, Institute for Biology II, Freiburg, Germany.
Thomas BrülsCEA, DRF, IG, Genoscope, Evry, France.
Nico JehmlichHelmholtz Centre for Environmental Research-UFZ, Department of Molecular Systems Biology, Leipzig, Germany.
Martin von BergenHelmholtz Centre for Environmental Research-UFZ, Department of Molecular Systems Biology, Leipzig, Germany.
Matthias BollUniversity of Freiburg, Institute for Biology II, Freiburg, Germany.
University of Freiburg · DEHelmholtz Centre for Environmental Research · DECommissariat à l'Énergie Atomique et aux Énergies Alternatives · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the past two decades, the study of oxygen-independent degradation of widely abundant aromatic compounds in anaerobic bacteria has revealed numerous unprecedented enzymatic principles. Surprisingly, the organisms, metabolites and enzymes involved in the degradation of o-phthalate (1,2-dicarboxybenzene), mainly derived from phthalate esters that are annually produced at the million ton scale, are sparsely known. Here, we demonstrate a previously unknown capacity of complete phthalate degradation in established aromatic compound-degrading, denitrifying model organisms of the genera Thauera, Azoarcus and 'Aromatoleum'. Differential proteome analyses revealed phthalate-induced gene clusters involved in uptake and conversion of phthalate to the central intermediate benzoyl-CoA. Enzyme assays provided in vitro evidence for the formation of phthaloyl-CoA by a succinyl-CoA- and phthalate-specific CoA transferase, which is essential for the subsequent oxygen-sensitive decarboxylation to benzoyl-CoA. The extreme instability of the phthaloyl-CoA intermediate requires highly balanced CoA transferase and decarboxylase activities to avoid its cellular accumulation. Phylogenetic analysis revealed phthaloyl-CoA decarboxylase as a novel member of the UbiD-like, (de)carboxylase enzyme family. Homologs of the encoding gene form a phylogenetic cluster and are found in soil, freshwater and marine bacteria; an ongoing global distribution of a possibly only recently evolved degradation pathway is suggested.

Indexed as

Acyl Coenzyme AAnaerobiosisBacteriaBacterial ProteinsBiodegradation, EnvironmentalCoenzyme A-TransferasesMultigene FamilyPhthalic AcidsPhylogenyAcyl Coenzyme ABacterial Proteinsbenzoyl-coenzyme ACoenzyme A-Transferasesphthalic acidPhthalic Acidssuccinyl-coenzyme A

Identifiers

PMID27392087
PMCPMC5315483
OpenAlexW2460308434

What OpenQuestion holds

Textmetadata
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.