Evidence map›Paper›PMID 34165649›Full record

ArticleAMB Express2021

A GH89 human α-N-acetylglucosaminidase (hNAGLU) homologue from gut microbe Bacteroides thetaiotaomicron capable of hydrolyzing heparosan oligosaccharides.

Xiaohong Yang, Xiaoxiao Yang, Hai Yu, Lan Na, Tamashree Ghosh, John B McArthur, Tsui-Fen Chou, Patricia Dickson, Xi Chen

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in AMB Express, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 94% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

9 authors at 6 institutions in 3 countries.

Xiaohong YangDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA, 95616, USA.
Xiaoxiao YangDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA, 95616, USA.
Hai YuDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA, 95616, USA.
Lan NaDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA, 95616, USA.
Tamashree GhoshDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA, 95616, USA.
John B McArthurDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA, 95616, USA.
Tsui-Fen ChouDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, 91125, USA.
Patricia DicksonDivision of Genetics and Genomic Medicine, Department of Pediatrics, Washington University School of Medicine, St. Louis, MO, 63110, USA.
Xi ChenDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA, 95616, USA. xiichen@ucdavis.edu.ORCID http://orcid.org/0000-0002-3160-614X
University of California, Davis · USCalifornia Institute of Technology · USResearch Institute for Chromatography · BERosalind Franklin Institute · GBUniversity of California System · USWashington University in St. Louis · US

Funding

Chemoenzymatic synthesis of bacterial polysaccharidesU01GM125288 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI KIESSLING, LAURA L, LI, LEI · 2017 to 2020
$3.1M
NIGMS NIH HHS U01 GM125288NIH HHS U01GM125288
6 · The paper itself

Abstract

Carbohydrate-Active enZYme (CAZY) GH89 family enzymes catalyze the cleavage of terminal α-N-acetylglucosamine from glycans and glycoconjugates. Although structurally and mechanistically similar to the human lysosomal α-N-acetylglucosaminidase (hNAGLU) in GH89 which is involved in the degradation of heparan sulfate in the lysosome, the reported bacterial GH89 enzymes characterized so far have no or low activity toward α-N-acetylglucosamine-terminated heparosan oligosaccharides, the preferred substrates of hNAGLU. We cloned and expressed several soluble and active recombinant bacterial GH89 enzymes in Escherichia coli. Among these enzymes, a truncated recombinant α-N-acetylglucosaminidase from gut symbiotic bacterium Bacteroides thetaiotaomicron ∆22Bt3590 was found to catalyze the cleavage of the terminal α1-4-linked N-acetylglucosamine (GlcNAc) from a heparosan disaccharide with high efficiency. Heparosan oligosaccharides with lengths up to decasaccharide were also suitable substrates. This bacterial α-N-acetylglucosaminidase could be a useful catalyst for heparan sulfate analysis.

Indexed as

Bacterial glycoside hydrolasesBacteroides thetaiotaomicronHeparosan oligosaccharidesNAGLUα-N-Acetylglucosaminidase

Identifiers

PMID34165649
PMCPMC8225759
OpenAlexW3176266930

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.