Evidence map›Paper›PMID 41561435›Full record

ArticleACS catalysis2026

Dual-Activity Mannosyltransferase Phosphorylases in Family 130 of Glycoside Hydrolases.

Simon Ladeveze, Laurence Tarquis, Gianluca Cioci, David Guieysse, Julien Durand, Régis Fauré, Ao Li, Jeremy Esque, Maxant Vivier, Yannick Malbert and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS catalysis, 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

12 authors.

Simon LadevezeTBI, Université de Toulouse, CNRS, INRAE, INSA, 31077 Toulouse, France.ORCID https://orcid.org/0000-0001-5062-3984
Laurence TarquisTBI, Université de Toulouse, CNRS, INRAE, INSA, 31077 Toulouse, France.
Gianluca CiociTBI, Université de Toulouse, CNRS, INRAE, INSA, 31077 Toulouse, France.ORCID https://orcid.org/0000-0001-6550-1672
David GuieysseTBI, Université de Toulouse, CNRS, INRAE, INSA, 31077 Toulouse, France.ORCID https://orcid.org/0000-0002-8802-4968
Julien DurandTBI, Université de Toulouse, CNRS, INRAE, INSA, 31077 Toulouse, France.
Régis FauréTBI, Université de Toulouse, CNRS, INRAE, INSA, 31077 Toulouse, France.
Ao LiTBI, Université de Toulouse, CNRS, INRAE, INSA, 31077 Toulouse, France.
Jeremy EsqueTBI, Université de Toulouse, CNRS, INRAE, INSA, 31077 Toulouse, France.
Maxant VivierTBI, Université de Toulouse, CNRS, INRAE, INSA, 31077 Toulouse, France.
Yannick MalbertSweeTech SAS, 31077 Toulouse, France.
Elisabeth LavilleTBI, Université de Toulouse, CNRS, INRAE, INSA, 31077 Toulouse, France.
Gabrielle Potocki-VeroneseTBI, Université de Toulouse, CNRS, INRAE, INSA, 31077 Toulouse, France.ORCID https://orcid.org/0000-0003-4232-230X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We discovered that certain mannoside-active enzymes from family GH130 possess both glycoside phosphorylase (GP) and weak glycosyltransferase (GT) activities. This dual activity was observed only in glycoside phosphorylases acting on β-(1,2)- and β-(1,3)-mannosides, being absent in β-(1,4)-mannoside phosphorylases. We provide several three-dimensional (3D) structures of β-(1,2)-mannosyltransferase phosphorylases Uhgb_MS (identified from the human gut microbiome (subfamily GH130_4)) and Teth514_1788 (from

Indexed as

carbohydrate-active enzymesglycoside hydrolaseglycoside phosphorylaseglycosyltransferasemannosides

Identifiers

PMID41561435
PMCPMC12814180

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.