Evidence map›Paper›PMID 24297170›Full record

ArticleThe Journal of biological chemistry2014

Understanding how the complex molecular architecture of mannan-degrading hydrolases contributes to plant cell wall degradation.

Xiaoyang Zhang, Artur Rogowski, Lei Zhao, Michael G Hahn, Utku Avci, J Paul Knox, Harry J Gilbert

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

26 citing papers in PubMed, 58 citations in OpenAlex.

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  10. A Possible Role of the Aleurone Expressed GeneFrontiers in plant science · 2019
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  11. Detection of Seasonal Variation inFrontiers in plant science · 2019
    Article
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  18. Article
  19. Article
  20. Review
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 at 2 institutions in 2 countries.

Xiaoyang ZhangFrom the Institute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Newcastle-upon-Tyne, NE 4HH, United Kingdom.
Artur Rogowski
Lei Zhao
Michael G Hahn
Utku Avci
J Paul Knox
Harry J Gilbert
Newcastle University · GBUniversity of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E015190/1Wellcome Trust 097907
6 · The paper itself

Abstract

Microbial degradation of plant cell walls is a central component of the carbon cycle and is of increasing importance in environmentally significant industries. Plant cell wall-degrading enzymes have a complex molecular architecture consisting of catalytic modules and, frequently, multiple non-catalytic carbohydrate binding modules (CBMs). It is currently unclear whether the specificities of the CBMs or the topology of the catalytic modules are the primary drivers for the specificity of these enzymes against plant cell walls. Here, we have evaluated the relationship between CBM specificity and their capacity to enhance the activity of GH5 and GH26 mannanases and CE2 esterases against intact plant cell walls. The data show that cellulose and mannan binding CBMs have the greatest impact on the removal of mannan from tobacco and Physcomitrella cell walls, respectively. Although the action of the GH5 mannanase was independent of the context of mannan in tobacco cell walls, a significant proportion of the polysaccharide was inaccessible to the GH26 enzyme. The recalcitrant mannan, however, was fully accessible to the GH26 mannanase appended to a cellulose binding CBM. Although CE2 esterases display similar specificities against acetylated substrates in vitro, only CjCE2C was active against acetylated mannan in Physcomitrella. Appending a mannan binding CBM27 to CjCE2C potentiated its activity against Physcomitrella walls, whereas a xylan binding CBM reduced the capacity of esterases to deacetylate xylan in tobacco walls. This work provides insight into the biological significance for the complex array of hydrolytic enzymes expressed by plant cell wall-degrading microorganisms.

Indexed as

BryopsidaCelluloseCell WallEsterasesGlycoside HydrolasesNicotianaPlant ProteinsXylansCelluloseEsterasesGlycoside HydrolasesPlant ProteinsXylansCarbohydrate-binding ProteinGlycoside HydrolasesMicroscopic ImagingPlant Cell WallPolysaccharide

Identifiers

PMID24297170
PMCPMC3900950
OpenAlexW2021484273

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.