Evidence map›Paper›PMID 29052930›Full record

ArticleEnvironmental microbiology2017

Comprehensive functional characterization of the glycoside hydrolase family 3 enzymes from Cellvibrio japonicus reveals unique metabolic roles in biomass saccharification.

Cassandra E Nelson, Mohamed A Attia, Artur Rogowski, Carl Morland, Harry Brumer, Jeffrey G Gardner

Open access · greenAbstract read
In one paragraph

Article in Environmental microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

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  11. Laminarin is a major molecule in the marine carbon cycle.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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  16. In vitro and in vivo characterization of threeBiotechnology for biofuels · 2018
    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

6 authors at 3 institutions in 3 countries.

Cassandra E NelsonDepartment of Biological Sciences, University of Maryland, Baltimore County, MD, USA.
Mohamed A AttiaMichael Smith Laboratories, University of British Columbia, Vancouver, Canada.
Artur RogowskiInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle Upon Tyne, UK.
Carl MorlandInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle Upon Tyne, UK.
Harry BrumerMichael Smith Laboratories, University of British Columbia, Vancouver, Canada.
Jeffrey G GardnerDepartment of Biological Sciences, University of Maryland, Baltimore County, MD, USA.ORCID http://orcid.org/0000-0001-6376-1219
Newcastle University · GBUniversity of British Columbia · CAUniversity of Maryland, Baltimore County · US

Funding

EXPAND PARTICIPATION BY MINORITIES IN BIOMEDICAL SCIENCER25GM055036 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI SUMMERS, MICHAEL FINLEY · 1996 to 2021
$16.9M
NIGMS NIH HHS R25 GM055036
6 · The paper itself

Abstract

Lignocellulose degradation is central to the carbon cycle and renewable biotechnologies. The xyloglucan (XyG), β(1→3)/β(1→4) mixed-linkage glucan (MLG) and β(1→3) glucan components of lignocellulose represent significant carbohydrate energy sources for saprophytic microorganisms. The bacterium Cellvibrio japonicus has a robust capacity for plant polysaccharide degradation, due to a genome encoding a large contingent of Carbohydrate-Active enZymes (CAZymes), many of whose specific functions remain unknown. Using a comprehensive genetic and biochemical approach, we have delineated the physiological roles of the four C. japonicus glycoside hydrolase family 3 (GH3) members on diverse β-glucans. Despite high protein sequence similarity and partially overlapping activity profiles on disaccharides, these β-glucosidases are not functionally equivalent. Bgl3A has a major role in MLG and sophorose utilization, and supports β(1→3) glucan utilization, while Bgl3B underpins cellulose utilization and supports MLG utilization. Bgl3C drives β(1→3) glucan utilization. Finally, Bgl3D is the crucial β-glucosidase for XyG utilization. This study not only sheds the light on the metabolic machinery of C. japonicus, but also expands the repertoire of characterized CAZymes for future deployment in biotechnological applications. In particular, the precise functional analysis provided here serves as a reference for informed bioinformatics on the genomes of other Cellvibrio and related species.

Indexed as

Amino Acid Sequencebeta-Glucansbeta-GlucosidaseBiomassCarbohydrate MetabolismCellvibrioGlucansGlycoside HydrolasesLigninXylansbeta-Glucansbeta-GlucosidaseGlucansGlycoside HydrolasesLigninlignocellulosesophoroseXylansxyloglucan

Identifiers

PMID29052930
PMCPMC5858740
OpenAlexW2765217010

What OpenQuestion holds

Textmetadata
LicenceTDM
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.