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Record W4409696593 · doi:10.1111/febs.70095

Structural and functional insights into extreme thermal stability and activity of two <scp>GH</scp> 12 domains of a multidomain glycosidase from a hyperthermophilic euryarchaeon

2025· article· en· W4409696593 on OpenAlexaff
Kseniya S. Zayulina, Evgenii N. Frolov, Christina Stracke, Alexandra A. Klyukina, Anna N. Khusnutdinova, P.J. Stogios, T. Skarina, Alexander F. Yakunin, Peter N. Golyshin, Bettina Siebers, Tatiana E. Shugaeva, Ilya V. Kublanov

Bibliographic record

VenueFEBS Journal · 2025
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicEnzyme Production and Characterization
Canadian institutionsUniversity of Toronto
FundersEuropean Regional Development FundMinistry of Science and Higher Education of the Russian FederationEuropean Commission
KeywordsThermostabilityGlycoside hydrolaseActive siteEnzymeBiochemistryCell wallThermophileCarbohydrate-binding modulePolysaccharideProtein engineeringPsychrophileCelluloseChemistryHydrolaseMutagenesisRecombinant DNAMutantXylanaseStereochemistry

Abstract

fetched live from OpenAlex

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 opt ) of 60 °C and 80 °C, respectively. The present study was focused on the characterization of two GH12 domains of the MDG. Purified recombinant TMDG_GH12‐1 and TMDG_GH12‐2 proteins were active as individual enzymes but exhibited distinct catalytic properties. Both enzymes were thermostable and active at extremely high temperatures: TMDG_GH12‐1 was active at 40–130 °C ( T opt 100 °C), and its half‐life ( t ½ ) at 100 °C was 42 h, which makes it one of the most thermostable glycosidases known so far, whereas TMDG_GH12‐2 was active at 50–100 °C ( T opt 90 °C) with t ½ at 100 °C being 30 min. Phylogenetic and structural analysis of both TMDG_GH12 proteins together with molecular docking and site‐directed mutagenesis suggested that the presence of two disulfide bridges and the W → Q mutation in the active site contribute to the exceptional thermostability of TMDG_GH12‐1. Further structural and mutational studies of the TMDG_GH12‐1 domain will help to gain a better understanding of the molecular mechanisms of its extraordinary thermostability and substrate specificity.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.302
Threshold uncertainty score0.411

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0000.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.016
GPT teacher head0.236
Teacher spread0.220 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one teacher head, not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations1
Published2025
Admission routes1
Has abstractyes

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