Evidence map›Paper›PMID 40259595›Full record

ArticleThe FEBS journal2025

Structural and functional insights into extreme thermal stability and activity of two GH12 domains of a multidomain glycosidase from a hyperthermophilic euryarchaeon.

Kseniya S Zayulina, Evgenii N Frolov, Christina Stracke, Alexandra A Klyukina, Anna N Khusnutdinova, Peter Stogios, Tatiana Skarina, Alexander F Yakunin, Peter N Golyshin, Bettina Siebers and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The FEBS journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

12 authors.

Kseniya S ZayulinaWinogradsky Institute of Microbiology, Federal Research Center of Biotechnology, Russian Academy of Sciences, Moscow, Russia.ORCID https://orcid.org/0000-0002-3748-0509
Evgenii N FrolovWinogradsky Institute of Microbiology, Federal Research Center of Biotechnology, Russian Academy of Sciences, Moscow, Russia.
Christina StrackeMolecular Enzyme Technology and Biochemistry, Environmental Microbiology and Biotechnology (EMB), Centre for Water and Environmental Research (CWE), Faculty of Chemistry, University of Duisburg-Essen, Germany.
Alexandra A KlyukinaWinogradsky Institute of Microbiology, Federal Research Center of Biotechnology, Russian Academy of Sciences, Moscow, Russia.
Anna N KhusnutdinovaCentre for Environmental Biotechnology, School of Environmental and Natural Sciences, Bangor University, UK.
Peter StogiosDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, Canada.ORCID https://orcid.org/0000-0001-8663-1425
Tatiana SkarinaDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, Canada.
Alexander F YakuninCentre for Environmental Biotechnology, School of Environmental and Natural Sciences, Bangor University, UK.ORCID https://orcid.org/0000-0003-0813-6490
Peter N GolyshinCentre for Environmental Biotechnology, School of Environmental and Natural Sciences, Bangor University, UK.
Bettina SiebersMolecular Enzyme Technology and Biochemistry, Environmental Microbiology and Biotechnology (EMB), Centre for Water and Environmental Research (CWE), Faculty of Chemistry, University of Duisburg-Essen, Germany.
Tatiana E ShugaevaDepartment of Bioengineering and Bioinformatics, Moscow State University, Russia.
Ilya V KublanovWinogradsky Institute of Microbiology, Federal Research Center of Biotechnology, Russian Academy of Sciences, Moscow, Russia.ORCID https://orcid.org/0000-0002-6845-8873

Funding

ERDF-Welsh Government co-funded CEB-Centre for Environmental Biotechnology Project 810280Horizon 2020 FuturEnzyme 10100032HotZyme 265933Ministry of Science and Higher Education of the Russian Federation
6 · The paper itself

Abstract

Bacteria and fungi are well known for efficient degradation of plant polysaccharides thanks to various enzymes involved in plant cell wall decomposition. However, little is known about the role of archaea in this process or the repertoire and features of their polysaccharide-degrading enzymes. In our previous work, we discovered an archaeal multidomain glycosidase (MDG) composed of three catalytic domains (GH5 and two GH12) and two cellulose-binding modules (CBM2). The recombinant MDG and individual GH5 catalytic domain were active against cellulose and a number of other polysaccharides at a wide range of temperatures, with optimum temperatures (T

Indexed as

Archaeal ProteinsGlycoside HydrolasesAmino Acid SequenceCatalytic DomainCelluloseEnzyme StabilityHot TemperatureKineticsModels, MolecularMutagenesis, Site-DirectedProtein DomainsRecombinant ProteinsSubstrate SpecificityTemperatureArchaeal ProteinsCelluloseGlycoside HydrolasesRecombinant Proteinscellulaseglycosidasehyperthermophilic archaeathermostabilitythermozymexylanase

Identifiers

PMID40259595
PMCPMC12265866

What OpenQuestion holds

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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.