Evidence map›Paper›PMID 25488985›Full record

ArticleGlycobiology2015

Enzymatic properties and subtle differences in the substrate specificity of phylogenetically distinct invertebrate N-glycan processing hexosaminidases.

Martin Dragosits, Shi Yan, Ebrahim Razzazi-Fazeli, Iain B H Wilson, Dubravko Rendic

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Glycobiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Analysis of Caenorhabditis Protein Glycosylation.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  3. Article
  4. Glycobiotechnology of the Insect Cell-Baculovirus Expression System Technology.Advances in biochemical engineering/biotechnology · 2021
    Article
  5. β-Hexosaminidases Along the Secretory Pathway ofFrontiers in plant science · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The underestimated N-glycomes of lepidopteran species.Biochimica et biophysica acta. General subjects · 2017
    Article
  11. Article
  12. Article
  13. Analysis of Invertebrate and Protist N-Glycans.Methods in molecular biology (Clifton, N.J.) · 2017
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors at 2 institutions in 1 country.

Martin DragositsDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna VetCore Facility for Research, University of Veterinary Medicine, Vienna, Austria.
Shi YanDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna.
Ebrahim Razzazi-FazeliVetCore Facility for Research, University of Veterinary Medicine, Vienna, Austria.
Iain B H WilsonDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna.
Dubravko RendicDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna dubravko.rendic@boku.ac.at.
BOKU University · ATUniversity of Veterinary Medicine Vienna · AT

Funding

Austrian Science Fund FWF P 23922Austrian Science Fund FWF TRP 127
6 · The paper itself

Abstract

Fused lobes (FDL) hexosaminidases are the most recently genetically defined glycosidases involved in the biosynthesis of N-glycans in invertebrates, and their narrow specificity is essential for the generation of paucimannosidic N-glycans in insects. In this study, we explored the potential of FDL hexosaminidases in the utilization of different artificial and natural substrates, both as purified, native compounds or generated in vitro using various relevant glycosyltransferases. In addition to the already-known FDL enzyme from Drosophila melanogaster, we now have identified and characterized the Apis mellifera FDL homolog. The enzymatic properties of the soluble forms of the affinity-purified insect FDL enzymes, expressed in both yeast and insect cells, were compared with those of the phylogenetically distinct recombinant Caenorhabditis elegans FDL-like enzymes and the N-acetylgalactosamine (GalNAc)-specific Caenorhabditis hexosaminidase HEX-4. In tests with a range of substrates, including natural N-glycans, we show that the invertebrate FDL(-like) enzymes are highly specific for N-acetylglucosamine attached to the α1,3-mannose, but under extreme conditions also remove other terminal GalNAc and N-acetylglucosamine residues. Recombinant FDL also proved useful in the analysis of complex mixtures of N-glycans originating from wild-type and mutant Caenorhabditis strains, thereby aiding isomeric definition of paucimannosidic and hybrid N-glycans in this organism. Furthermore, differences in activity and specificity were shown for two site-directed mutants of Drosophila FDL, compatible with the high structural similarity of chitinolytic and N-glycan degrading exohexosaminidases in insects. Our studies are another indication for the variety of structural and function aspects in the GH20 hexosaminidase family important for both catabolism and biosynthesis of glycoconjugates in eukaryotes.

Indexed as

Amino Acid SequenceAnimalsBeesBiocatalysisCaenorhabditis elegansCaenorhabditis elegans ProteinsCarbohydrate ConformationCarbohydrate SequenceCell LineDrosophila melanogasterDrosophila ProteinsGlycopeptidesGlycosylationHexosaminidasesHydrogen-Ion ConcentrationMolecular Sequence DataCaenorhabditis elegans ProteinsDrosophila ProteinsGlycopeptidesHexosaminidasesPolysaccharidesfused lobeshexosaminidaseinsectinvertebrateN-glycans

Identifiers

PMID25488985
PMCPMC4339880
OpenAlexW2134831951

What OpenQuestion holds

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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.