Evidence map›Paper›PMID 30514885›Full record

ArticleScientific reports2018

The LPG1x family from Leishmania major is constituted of rare eukaryotic galactofuranosyltransferases with unprecedented catalytic properties.

Jihen Ati, Cyril Colas, Pierre Lafite, Ryan P Sweeney, Ruixiang Blake Zheng, Todd L Lowary, Richard Daniellou

Abstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Galactofuranose-Related Enzymes: Challenges and Hopes.International journal of molecular sciences · 2020
    Review
  5. 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

7 authors.

Jihen AtiInstitut de Chimie Organique et Analytique, UMR CNRS 7311, Université d'Orléans, Rue de Chartres, BP6759, Orléans, Cedex 02, France.
Cyril ColasInstitut de Chimie Organique et Analytique, UMR CNRS 7311, Université d'Orléans, Rue de Chartres, BP6759, Orléans, Cedex 02, France.
Pierre LafiteInstitut de Chimie Organique et Analytique, UMR CNRS 7311, Université d'Orléans, Rue de Chartres, BP6759, Orléans, Cedex 02, France.ORCID http://orcid.org/0000-0003-1637-4966
Ryan P SweeneyAlberta Glycomics Centre and Department of Chemistry, The University of Alberta, Edmonton, AB, T6G 2G2, Canada.
Ruixiang Blake ZhengAlberta Glycomics Centre and Department of Chemistry, The University of Alberta, Edmonton, AB, T6G 2G2, Canada.
Todd L LowaryAlberta Glycomics Centre and Department of Chemistry, The University of Alberta, Edmonton, AB, T6G 2G2, Canada.ORCID http://orcid.org/0000-0002-8331-8211
Richard DaniellouInstitut de Chimie Organique et Analytique, UMR CNRS 7311, Université d'Orléans, Rue de Chartres, BP6759, Orléans, Cedex 02, France. richard.daniellou@univ-orleans.fr.ORCID http://orcid.org/0000-0001-7296-3736

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Galactofuranosyltransferases are poorly described enzymes despite their crucial role in the virulence and the pathogenicity of numerous microorganisms. These enzymes are considered as potential targets for therapeutic action. In addition to the only well-characterised prokaryotic GlfT2 from Mycobacterium tuberculosis, four putative genes in Leishmania major were previously described as potential galactofuranosyltransferases. In this study, we have cloned, over-expressed, purified and fully determined the kinetic parameters of these four eukaryotic enzymes, thus demonstrating their unique potency in catalysing the transfer of the galactofuranosyl moiety into acceptors. Their individual promiscuity revealed to be different, as some of them could efficiently use NDP-pyranoses as donor substrates in addition to the natural UDP-galactofuranose. Such results pave the way for the development of chemoenzymatic synthesis of furanosyl-containing glycoconjugates as well as the design of improved drugs against leishmaniasis.

Indexed as

BiocatalysisEscherichia coliGalactoseGalactosyltransferasesKineticsLeishmania majorProtozoan ProteinsSubstrate SpecificityUridine DiphosphateGalactoseGalactosyltransferasesLPG1 protein, LeishmaniaProtozoan ProteinsUridine Diphosphateuridine diphosphate galactofuranose

Identifiers

PMID30514885
PMCPMC6279836

What OpenQuestion holds

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Registered trials

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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.