Evidence map›Paper›PMID 31905894›Full record

ArticleMarine drugs2019

Elucidation of a Unique Pattern and the Role of Carbohydrate Binding Module of an Alginate Lyase.

Fu Hu, Benwei Zhu, Qian Li, Heng Yin, Yun Sun, Zhong Yao, Dengming Ming

Abstract read
In one paragraph

Article in Marine drugs, 2019. 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
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Effects of Module Truncation of a New Alginate Lyase VxAly7C from MarineInternational journal of molecular sciences · 2022
    Article
  10. Review
  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

7 authors.

Fu HuCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing 211816, China.
Benwei ZhuCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing 211816, China.ORCID 0000-0001-5692-8535
Qian LiCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing 211816, China.
Heng YinDalian Institute of Chemical Physics, Chinese Academy of Sciences, CAS, Dalian 116023, China.
Yun SunCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing 211816, China.
Zhong YaoCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing 211816, China.
Dengming MingCollege of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing 211816, China.ORCID 0000-0002-5566-9778

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alginate oligosaccharides with different degrees of polymerization (DPs) possess diverse physiological activities. Therefore, in recent years, increasing attention has been drawn to the use of enzymes for the preparation of alginate oligosaccharides for food and industrial applications. Previously, we identified and characterized a novel bifunctional alginate lyase Aly7A, which can specifically release trisaccharide from three different substrate types with a unique degradation pattern. Herein, we investigated its degradation pattern by modular truncation and molecular docking. The results suggested that Aly7A adopted a unique action mode towards different substrates with the substrate chain sliding into the binding pocket of the catalytic domain to position the next trisaccharide for cleavage. Deletion of the Aly7A carbohydrate binding module (CBM) domain resulted in a complex distribution of degradation products and no preference for trisaccharide formation, indicating that the CBM may act as a "controller" during the trisaccharide release process. This study further testifies CBM as a regulator of product distribution and provides new insights into well-defined generation of alginate oligosaccharides with associated CBMs.

Indexed as

Carbohydrate MetabolismMolecular Docking SimulationOligosaccharidesPolymerizationPolysaccharide-LyasesOligosaccharidespoly(beta-D-mannuronate) lyasePolysaccharide-Lyasesalginate lyasedegrading patternoligosaccharidestrisaccharide preparationunique mechanism

Identifiers

PMID31905894
PMCPMC7024192

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.