Evidence map›Paper›PMID 10781549›Full record

ArticleJournal of bacteriology2000

Characterization of an extracellular lipase encoded by LIP2 in Yarrowia lipolytica.

G Pignède, H Wang, F Fudalej, C Gaillardin, M Seman, J M Nicaud

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

48 citing papers in PubMed, 240 citations in OpenAlex.

  1. Review
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  8. Application of a New Engineered Strain ofInternational journal of molecular sciences · 2021
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  14. Review
  15. Article
  16. High-Level Production of a Thermostable Mutant ofInternational journal of molecular sciences · 2019
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  18. Noncovalent Immobilization ofBiomolecules · 2019
    Article
  19. Cellular and metabolic engineering of oleaginous yeastEngineering in life sciences · 2019
    Review
  20. Review
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 3 institutions in 1 country.

G PignèdeLaboratoire Mayoly Spindler, Service Recherche, 78401 Chatou Cedex, France.
H Wang
F Fudalej
C Gaillardin
M Seman
J M Nicaud
Mayoly Spindler (France) · FRLaboratoire de Microbiologie et Génétique Moléculaires · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We isolated the LIP2 gene from the lipolytic yeast Yarrowia lipolytica. It was found to encode a 334-amino-acid precursor protein. The secreted lipase is a 301-amino-acid glycosylated polypeptide which is a member of the triacylglycerol hydrolase family (EC 3.1.1.3). The Lip2p precursor protein is processed by the KEX2-like endoprotease encoded by XPR6. Deletion of the XPR6 gene resulted in the secretion of an active but less stable proenzyme. Thus, the pro region does not inhibit lipase secretion and activity. However, it does play an essential role in the production of a stable enzyme. Processing was found to be correct in LIP2(A) (multiple LIP2 copy integrant)-overexpressing strains, which secreted 100 times more activity than the wild type, demonstrating that XPR6 maturation was not limiting. No extracellular lipase activity was detected with the lip2 knockout (KO) strain, strongly suggesting that extracellular lipase activity results from expression of the LIP2 gene. Nevertheless, the lip2 KO strain is still able to grow on triglycerides, suggesting an alternative pathway for triglyceride utilization in Y. lipolytica.

Indexed as

Fungal ProteinsAmino Acid SequenceAnimalsBacterial ProteinsBase SequenceCulture MediaDNA, FungalGene ExpressionGenes, FungalGenetic VectorsGlycosylationLipaseMolecular Sequence DataProtein Processing, Post-TranslationalRabbitsSaccharomycetalesBacterial ProteinsCulture MediaDNA, FungalFungal ProteinsLIP2 protein, Yarrowia lipolyticaLipaseSerine EndopeptidasesTriglyceridesXPR6 protein, Yarrowia lipolytica

Identifiers

PMID10781549
PMCPMC101989
OpenAlexW2165360475

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.