Evidence map›Paper›PMID 38747981›Full record

ArticleApplied microbiology and biotechnology2024

Exploration of three Dyadobacter fermentans enzymes uncovers molecular activity determinants in CE15.

Miriam Carbonaro, Scott Mazurkewich, Gabriella Fiorentino, Leila Lo Leggio, Johan Larsbrink

Abstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2024. 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

5 authors.

Miriam Carbonaro *Department of Biology, University of Naples Federico II, 80126, Naples, Italy.
Scott Mazurkewich *Wallenberg Wood Science Center, Division of Industrial Biotechnology, Department of Life Sciences, Chalmers University of Technology, SE-412 96, Gothenburg, Sweden. scott.mazurkewich@chalmers.se.
Gabriella FiorentinoDepartment of Biology, University of Naples Federico II, 80126, Naples, Italy.
Leila Lo LeggioDepartment of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100, Copenhagen, Denmark.
Johan LarsbrinkWallenberg Wood Science Center, Division of Industrial Biotechnology, Department of Life Sciences, Chalmers University of Technology, SE-412 96, Gothenburg, Sweden. johan.larsbrink@chalmers.se.ORCID http://orcid.org/0000-0001-8386-2914

Funding

Knut och Alice Wallenbergs Stiftelse Wallenberg Wood Science CenterNovo Nordisk Fonden NNF21OC0071611
6 · The paper itself

Abstract

Glucuronoyl esterases (GEs) are serine-type hydrolase enzymes belonging to carbohydrate esterase family 15 (CE15), and they play a central role in the reduction of recalcitrance in plant cell walls by cleaving ester linkages between glucuronoxylan and lignin in lignocellulose. Recent studies have suggested that bacterial CE15 enzymes are more heterogeneous in terms of sequence, structure, and substrate preferences than their fungal counterparts. However, the sequence space of bacterial GEs has still not been fully explored, and further studies on diverse enzymes could provide novel insights into new catalysts of biotechnological interest. To expand our knowledge on this family of enzymes, we investigated three unique CE15 members encoded by Dyadobacter fermentans NS114

Indexed as

Zea maysBacterial ProteinsEsterasesLigninPhylogenySubstrate SpecificityBacterial ProteinsEsterasesLigninBiomassDyadobacterGlucuronoyl esteraseHydrolaseLignocellulose

Identifiers

PMID38747981
PMCPMC11096219

What OpenQuestion holds

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Registered trials

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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.