Evidence map›Paper›PMID 29240834›Full record

ArticlePloS one2017

Discovery of carbamate degrading enzymes by functional metagenomics.

Lisa Ufarté, Elisabeth Laville, Sophie Duquesne, Diego Morgavi, Patrick Robe, Christophe Klopp, Angeline Rizzo, Sandra Pizzut-Serin, Gabrielle Potocki-Veronese

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Microbial plastic degradation: enzymes, pathways, challenges, and perspectives.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
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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 6 institutions in 1 country.

Lisa UfartéLISBP, Université de Toulouse, CNRS, INRA, INSA, Toulouse, France.
Elisabeth LavilleLISBP, Université de Toulouse, CNRS, INRA, INSA, Toulouse, France.
Sophie DuquesneLISBP, Université de Toulouse, CNRS, INRA, INSA, Toulouse, France.
Diego MorgaviUMRH, INRA, Vetagro Sup, France.
Patrick RobeLibraGen S.A., Toulouse, France.
Christophe KloppPlateforme Bio-informatique Toulouse Genopole, UBIA INRA, Castanet-Tolosan, France.
Angeline RizzoLISBP, Université de Toulouse, CNRS, INRA, INSA, Toulouse, France.
Sandra Pizzut-SerinLISBP, Université de Toulouse, CNRS, INRA, INSA, Toulouse, France.
Gabrielle Potocki-VeroneseLISBP, Université de Toulouse, CNRS, INRA, INSA, Toulouse, France.
Centre National de la Recherche Scientifique · FRInstitut National des Sciences Appliquées de Toulouse · FRGénétique Physiologie et Systèmes d'Elevage · FRLaboratoire d'Ingénierie des Systèmes Biologiques et des Procédés · FRUniversité Fédérale de Toulouse Midi-Pyrénées · FRVetAgro Sup · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bioremediation of pollutants is a major concern worldwide, leading to the research of new processes to break down and recycle xenobiotics and environment contaminating polymers. Among them, carbamates have a very broad spectrum of uses, such as toxinogenic pesticides or elastomers. In this study, we mined the bovine rumen microbiome for carbamate degrading enzymes. We isolated 26 hit clones exhibiting esterase activity, and were able to degrade at least one of the targeted polyurethane and pesticide carbamate compounds. The most active clone was deeply characterized. In addition to Impranil, this clone was active on Tween 20, pNP-acetate, butyrate and palmitate, and on the insecticide fenobucarb. Sequencing and sub-cloning of the best target revealed a novel carboxyl-ester hydrolase belonging to the lipolytic family IV, named CE_Ubrb. This study highlights the potential of highly diverse microbiota such as the ruminal one for the discovery of promiscuous enzymes, whose versatility could be exploited for industrial uses.

Indexed as

MetagenomicsAnimalsCarbamatesCattleCarbamates

Identifiers

PMID29240834
PMCPMC5730166
OpenAlexW2775152656

What OpenQuestion holds

Textmetadata
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.