Evidence map›Paper›PMID 33838183›Full record

ArticleThe Journal of biological chemistry

Functional diversity of three tandem C-terminal carbohydrate-binding modules of a β-mannanase.

Marie Sofie Møller, Souad El Bouaballati, Bernard Henrissat, Birte Svensson

Abstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Article
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  5. Article
  6. Structural and enzymatic characterization of the sialidase SiaPG from Porphyromonas gingivalis.Acta crystallographica. Section F, Structural biology communications · 2023
    Article
  7. Article
  8. Article
  9. Whole genome sequence ofFrontiers in microbiology · 2023
    Article
  10. Article
  11. 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

4 authors.

Marie Sofie MøllerDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Lyngby, Denmark. Electronic address: msmo@dtu.dk.
Souad El BouaballatiDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Lyngby, Denmark.
Bernard HenrissatArchitecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université, Marseille, France; Department of Biological Sciences, King Abdulaziz University, Jeddah, Saudi Arabia.
Birte SvenssonDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Lyngby, Denmark.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbohydrate active enzymes, such as those involved in plant cell wall and storage polysaccharide biosynthesis and deconstruction, often contain repeating noncatalytic carbohydrate-binding modules (CBMs) to compensate for low-affinity binding typical of protein-carbohydrate interactions. The bacterium Saccharophagus degradans produces an endo-β-mannanase of glycoside hydrolase family 5 subfamily 8 with three phylogenetically distinct family 10 CBMs located C-terminally from the catalytic domain (SdGH5_8-CBM10x3). However, the functional roles and cooperativity of these CBM domains in polysaccharide binding are not clear. To learn more, we studied the full-length enzyme, three stepwise CBM family 10 (CBM10) truncations, and GFP fusions of the individual CBM10s and all three domains together by pull-down assays, affinity gel electrophoresis, and activity assays. Only the C-terminal CBM10-3 was found to bind strongly to microcrystalline cellulose (dissociation constant, K

Indexed as

Amino Acid Sequencebeta-MannosidaseCatalytic DomainCelluloseGalactoseGammaproteobacteriaMannansProtein ConformationSequence HomologySubstrate Specificity(1-6)-alpha-glucomannanbeta-MannosidaseCellulosegalactomannanGalactoseMannansaffinity gel electrophoresisenzyme kineticsgalactomannanGFP–domain fusionglucomannanmannanmultimodular enzyme truncationprotein–carbohydrate interactionpull-down assayssubstrate specificity

Identifiers

PMID33838183
PMCPMC8121702

What OpenQuestion holds

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Registered trials

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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.