Evidence map›Paper›PMID 41760362›Full record

ArticleThe FEBS journal2026

Elucidating the catalytic mechanism of a previously undescribed carbohydrate esterase family 7 acetyl xylan esterase (LaCE7A).

Ang Lv, Junwen Ma, Ling Wang, Chu Wang, Qiaojuan Yan, Weiwei Han, Zhengqiang Jiang, Shaoqing Yang

Abstract read
In one paragraph

Article in The FEBS journal, 2026. 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

8 authors.

Ang LvCollege of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China.
Junwen MaKey Laboratory of Food Bioengineering (China National Light Industry), College of Engineering, China Agricultural University, Beijing, China.
Ling WangCollege of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China.
Chu WangKey Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Science, Jilin University, Changchun, China.
Qiaojuan YanKey Laboratory of Food Bioengineering (China National Light Industry), College of Engineering, China Agricultural University, Beijing, China.
Weiwei HanKey Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Science, Jilin University, Changchun, China.
Zhengqiang JiangCollege of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China.
Shaoqing YangCollege of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China.ORCID https://orcid.org/0000-0002-8708-677X

Funding

National Key Research and Development Program of China 2022YFD2101400
6 · The paper itself

Abstract

Acetyl xylan esterases (AcXEs) are crucial for biomass degradation. However, the catalytic mechanism underlying the highly specific activity remains poorly understood, limiting their rational engineering. Here, we characterized the previously undescribed carbohydrate esterase family (CE) 7 acetyl xylan esterase (LaCE7A) from Lactococcus lactis with high specific activity (154 179 U·mg

Indexed as

AcetylesteraseBacterial ProteinsLactococcus lactisAmino Acid SequenceBiocatalysisCatalysisCatalytic DomainKineticsModels, MolecularMolecular Dynamics SimulationRecombinant ProteinsSubstrate SpecificityAcetylesteraseacetylxylan esteraseBacterial ProteinsRecombinant Proteinsactive pocketAcXEsbiochemical characterizationcrystal structuretight turn region

Identifiers

PMID41760362
PMCPMC13370729

What OpenQuestion holds

Textmetadata
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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.