Evidence map›Paper›PMID 34684901›Full record

ArticleMolecules (Basel, Switzerland)2021

Discovery of a Kojibiose Hydrolase by Analysis of Specificity-Determining Correlated Positions in Glycoside Hydrolase Family 65.

Emma De Beul, Alana Jongbloet, Jorick Franceus, Tom Desmet

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Discovery of a Thermostable Nigerose Phosphorylase for the Efficient Chemoenzymatic Radiosynthesis of aJournal of nuclear medicine : official publication, Society of Nuclear Medicine · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.International journal of molecular sciences · 2022
    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

4 authors at 1 institution in 1 country.

Emma De BeulCentre for Synthetic Biology (CSB), Department of Biotechnology, Ghent University, Coupure Links 653, 9000 Ghent, Belgium.ORCID 0000-0002-9593-3182
Alana JongbloetCentre for Synthetic Biology (CSB), Department of Biotechnology, Ghent University, Coupure Links 653, 9000 Ghent, Belgium.
Jorick FranceusCentre for Synthetic Biology (CSB), Department of Biotechnology, Ghent University, Coupure Links 653, 9000 Ghent, Belgium.ORCID 0000-0003-4377-5933
Tom DesmetCentre for Synthetic Biology (CSB), Department of Biotechnology, Ghent University, Coupure Links 653, 9000 Ghent, Belgium.ORCID 0000-0002-5788-3022
Ghent University · BE

Funding

Research Foundation - Flanders 1S17721N
6 · The paper itself

Abstract

The Glycoside Hydrolase Family 65 (GH65) is an enzyme family of inverting α-glucoside phosphorylases and hydrolases that currently contains 10 characterized enzyme specificities. However, its sequence diversity has never been studied in detail. Here, an in-silico analysis of correlated mutations was performed, revealing specificity-determining positions that facilitate annotation of the family's phylogenetic tree. By searching these positions for amino acid motifs that do not match those found in previously characterized enzymes from GH65, several clades that may harbor new functions could be identified. Three enzymes from across these regions were expressed in

Indexed as

Amino Acid MotifsBacteroidetesDisaccharidesEscherichia coliGlycoside HydrolasesPhosphorylasesPhylogenySubstrate SpecificityDisaccharidesGlycoside HydrolaseskojibiosePhosphorylasesCMAcorrelated positionsGlycoside Hydrolase Family 65glycoside hydrolasesglycoside phosphorylaseskojibiasekojibiose glucohydrolasespecificity determinants

Identifiers

PMID34684901
PMCPMC8537180
OpenAlexW3205476802

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.