Evidence map›Paper›PMID 26580812›Full record

ArticlePloS one2015

Comprehensive Analysis of a Yeast Lipase Family in the Yarrowia Clade.

Muchalin Meunchan, Stéphanie Michely, Hugo Devillers, Jean-Marc Nicaud, Alain Marty, Cécile Neuvéglise

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

14 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  4. International journal of molecular sciences · 2023
    Article
  5. Review
  6. Comparative Analysis of the Alkaline Proteolytic Enzymes ofInternational journal of molecular sciences · 2023
    Article
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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

6 authors at 2 institutions in 2 countries.

Muchalin MeunchanUniversité de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077, Toulouse, France.
Stéphanie MichelyINRA, UMR 1319 Micalis, F-78352, Jouy-en-Josas, France.
Hugo DevillersINRA, UMR 1319 Micalis, F-78352, Jouy-en-Josas, France.
Jean-Marc NicaudINRA, UMR 1319 Micalis, F-78352, Jouy-en-Josas, France.
Alain MartyUniversité de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077, Toulouse, France.
Cécile NeuvégliseINRA, UMR 1319 Micalis, F-78352, Jouy-en-Josas, France.
AgroParisTech · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipases are currently the subject of intensive studies due to their large range of industrial applications. The Lip2p lipase from the yeast Yarrowia lipolytica (YlLIP2) was recently shown to be a good candidate for different biotechnological applications. Using a combination of comparative genomics approaches based on sequence similarity, synteny conservation, and phylogeny, we constructed the evolutionary scenario of the lipase family for six species of the Yarrowia clade. RNA-seq based transcriptome analysis revealed the primary role of LIP2 homologues in the assimilation of different substrates. Once identified, these YlLIP2 homologues were expressed in Y. lipolytica. The lipase Lip2a from Candida phangngensis was shown to naturally present better activity and enantioselectivity than YlLip2. Enantioselectivity was further improved by site-directed mutagenesis targeted to the substrate binding site. The mono-substituted variant V232S displayed enantioselectivity greater than 200 and a 2.5 fold increase in velocity. A double-substituted variant 97A-V232F presented reversed enantioselectivity, with a total preference for the R-enantiomer.

Indexed as

Evolution, MolecularPhylogenyTranscriptomeAmino Acid SequenceBinding SitesButyratesCandidaFungal ProteinsGene ExpressionHydrolysisIndustrial MicrobiologyLipaseMolecular Sequence DataMutagenesis, Site-DirectedProtein BindingSequence Alignment4-nitrophenyl butyrateButyratesFungal ProteinsLIP2 protein, Yarrowia lipolyticaLipase

Identifiers

PMID26580812
PMCPMC4651352
OpenAlexW2178650539

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.