Evidence map›Paper›PMID 29057942›Full record

ArticleScientific reports2017

Functional and Structural Studies of a Multidomain Alginate Lyase from Persicobacter sp. CCB-QB2.

Pei-Fang Sim, Go Furusawa, Aik-Hong Teh

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

18 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Effects of Module Truncation of a New Alginate Lyase VxAly7C from MarineInternational journal of molecular sciences · 2022
    Article
  9. Review
  10. Article
  11. Review
  12. Genome-Wide Analysis of PL7 Alginate Lyases in the GenusMolecules (Basel, Switzerland) · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Adaptations ofFrontiers in microbiology · 2019
    Article
  18. 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

3 authors at 1 institution in 1 country.

Pei-Fang SimCentre for Chemical Biology, Universiti Sains Malaysia, 10 Persiaran Bukit Jambul, 11900, Bayan Lepas, Penang, Malaysia.
Go FurusawaCentre for Chemical Biology, Universiti Sains Malaysia, 10 Persiaran Bukit Jambul, 11900, Bayan Lepas, Penang, Malaysia.
Aik-Hong TehCentre for Chemical Biology, Universiti Sains Malaysia, 10 Persiaran Bukit Jambul, 11900, Bayan Lepas, Penang, Malaysia. aikhong@usm.my.ORCID 0000-0001-6365-574X
Universiti Sains Malaysia · MY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AlyQ from Persicobacter sp. CCB-QB2 is an alginate lyase with three domains - a carbohydrate-binding domain modestly resembling family 16 carbohydrate-binding module (CBM16), a family 32 CBM (CBM32) domain, and an alginate lyase domain belonging to polysaccharide lyase family 7 (PL7). Although AlyQ can also act on polyguluronate (poly-G) and polymannuronate (poly-M), it is most active on alginate. Studies with truncated AlyQ showed that the CBM32 domain did not contribute to enhancing AlyQ's activity under the assayed conditions. Nevertheless, it could bind to cleaved but not intact alginate, indicating that the CBM32 domain recognises alginate termini. The crystal structure containing both CBM32 and catalytic domains show that they do not interact with one another. The CBM32 domain contains a conserved Arg that may bind to the carboxyl group of alginate. The catalytic domain, meanwhile, shares a conserved substrate-binding groove, and the presence of two negatively charged Asp residues may dictate substrate specificity especially at subsite +1. As Persicobacter sp. CCB-QB2 was unable to utilise alginate, AlyQ may function to help the bacterium degrade cell walls more efficiently.

Indexed as

AlginatesAmino Acid SequenceBacterial ProteinsBacteroidetesCatalytic DomainEscherichia coliKineticsPolysaccharide-LyasesProtein ConformationAlginatesBacterial Proteinspoly(beta-D-mannuronate) lyasePolysaccharide-Lyases

Identifiers

PMID29057942
PMCPMC5651945
OpenAlexW2767094899

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.