Evidence map›Paper›PMID 31698702›Full record

ReviewInternational journal of molecular sciences2019

β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides.

Ali Rohman, Bauke W Dijkstra, Ni Nyoman Tri Puspaningsih

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
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  12. The catabolic specialization of the marine bacteriumApplied and environmental microbiology · 2024
    Article
  13. Lactate cross-feeding betweenApplied and environmental microbiology · 2024
    Article
  14. Deleting an xylosidase-encoding geneFrontiers in microbiology · 2024
    Article
  15. Transcriptomic analysis of Chinese yam (Frontiers in nutrition · 2023
    Article
  16. Whole genome sequencing and annotation ofFrontiers in bioengineering and biotechnology · 2023
    Article
  17. β-Xylosidase SRBX1 Activity fromJournal of fungi (Basel, Switzerland) · 2022
    Article
  18. International journal of molecular sciences · 2022
    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

3 authors at 2 institutions in 2 countries.

Ali RohmanDepartment of Chemistry, Faculty of Science and Technology, Universitas Airlangga, Surabaya 60115, Indonesia.ORCID 0000-0002-8177-5881
Bauke W DijkstraLaboratory of Biophysical Chemistry, University of Groningen, 9747 AG Groningen, The Netherlands.ORCID 0000-0001-9731-6586
Ni Nyoman Tri PuspaningsihDepartment of Chemistry, Faculty of Science and Technology, Universitas Airlangga, Surabaya 60115, Indonesia.
Airlangga University · IDUniversity of Groningen · NL

Funding

Universitas Airlangga Hibah Riset Mandat No. 624/UN3.14/LT/2017Universitas Airlangga Tahir Professorship SK Rektor Unair No. 1149/UN3/2018
6 · The paper itself

Abstract

Xylan, a prominent component of cellulosic biomass, has a high potential for degradation into reducing sugars, and subsequent conversion into bioethanol. This process requires a range of xylanolytic enzymes. Among them, β-xylosidases are crucial, because they hydrolyze more glycosidic bonds than any of the other xylanolytic enzymes. They also enhance the efficiency of the process by degrading xylooligosaccharides, which are potent inhibitors of other hemicellulose-/xylan-converting enzymes. On the other hand, the β-xylosidase itself is also inhibited by monosaccharides that may be generated in high concentrations during the saccharification process. Structurally, β-xylosidases are diverse enzymes with different substrate specificities and enzyme mechanisms. Here, we review the structural diversity and catalytic mechanisms of β-xylosidases, and discuss their inhibition by monosaccharides.

Indexed as

BiocatalysisCatalytic DomainModels, MolecularMonosaccharidesXylansXylosidasesexo-1,4-beta-D-xylosidaseMonosaccharidesXylansXylosidasesbioethanolbiomassglycoside hydrolasehemicellulasehemicellulosexylanolytic enzyme

Identifiers

PMID31698702
PMCPMC6887791
OpenAlexW2987139837

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.