Evidence map›Paper›PMID 17006639›Full record

ArticleGlycoconjugate journal2006

Kinetic properties and substrate specificities of two recombinant human N-acetylglucosaminyltransferase-IV isozymes.

Suguru Oguri, Aruto Yoshida, Mari T Minowa, Makoto Takeuchi

Abstract read
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In one paragraph

Article in Glycoconjugate journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

23 citing papers in PubMed, 43 citations in OpenAlex.

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  13. N-Glycosylation.Advances in experimental medicine and biology · 2021
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  15. 3D Structure and Function of Glycosyltransferases Involved inInternational journal of molecular sciences · 2020
    Review
  16. Article
  17. Article
  18. Review
  19. 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

4 authors at 2 institutions in 1 country.

Suguru OguriDepartment of Bioproduction, Faculty of Bioindustry, Tokyo University of Agriculture, 196 Yasaka, Abashiri, Hokkaido, 099-2493, Japan. s-oguri@bioindustry.nodai.ac.jp
Aruto Yoshida
Mari T Minowa
Makoto Takeuchi
Kirin (Japan) · JPTokyo University of Agriculture · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-acetylglucosaminyltransferase (GnT)-IV catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-glycans. Two human GnT-IV isozymes (GnT-IVa and GnT-IVb) had been identified, which exhibit different expression profiles among human tissues and cancer cell lines. To clarify the enzymatic properties of the respective enzymes, their kinetic parameters were determined using recombinant full-length enzymes expressed in COS7 cells. The K (m) of human GnT-IVb for UDP-GlcNAc was estimated to be 0.24 mM, which is 2-fold higher than that of human GnT-IVa. The K (m) values of GnT-IVb for pyridylaminated (PA) acceptor sugar chains with different branch numbers were 3- to 6-fold higher than those of GnT-IVa. To compare substrate specificities more precisely, we generated recombinant soluble enzymes of human GnT-IVa and GnT-IVb with N-terminal flag tags. Both enzymes showed similar substrate specificities as determined using fourteen PA-sugar chains. They preferred complex-type N-glycans over hybrid-types. Among the complex-type N-glycans tested, the relative activities of both enzymes were increased in proportion to the number of GlcNAc branches on the Man alpha1-6 arm. The Man alpha1-6 arm of the acceptors was not essential for their activities because a linear pentasaccharide lacking this arm, GlcNAcbeta1-2Manalpha1-3Manbeta1-4GlcNAcbeta1-4 GlcNAc-PA, was a substrate for both enzymes. These results indicate that human GnT-IVb exhibits the same acceptor substrate specificities as human GnT-IVa, although GnT-IVb has lower affinities for donors or acceptors than GnT-IVa. This suggests that GnT-IVa is more active than GnT-IVb under physiological conditions and that it primarily contributes to the biosynthesis of N-glycans.

Indexed as

AnimalsCarbohydrate SequenceChlorocebus aethiopsCOS CellsHumansIsoenzymesKineticsMolecular Sequence DataN-AcetylglucosaminyltransferasesOligosaccharidesPolysaccharidesRecombinant ProteinsSubstrate Specificityalpha-1,3-mannosylglycoprotein beta-1,4-N-acetylglucosaminyltransferaseIsoenzymesN-AcetylglucosaminyltransferasesOligosaccharidesPolysaccharidesRecombinant Proteins

Identifiers

PMID17006639
OpenAlexW1987696840

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.