Evidence map›Paper›PMID 40529184›Full record

ArticleComputational and structural biotechnology journal2025

Protein flexibility drives sugar rotation and high substrate promiscuity in a GDP-sugar 4-epimerase.

Carlos Josué Alvarez Quispe, Koen Beerens, Andy-Mark W H Thunnissen, Xevi Biarnés, Antoni Planas, Tom Desmet

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Computational and structural biotechnology journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

6 authors.

Carlos Josué Alvarez QuispeCentre for Synthetic Biology (CSB), Department of Biotechnology, Ghent University, Coupure Links 653, Ghent 9000, Belgium.
Koen BeerensCentre for Synthetic Biology (CSB), Department of Biotechnology, Ghent University, Coupure Links 653, Ghent 9000, Belgium.
Andy-Mark W H ThunnissenGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, Groningen 9747 AG, the Netherlands.
Xevi BiarnésLaboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull, Via Augusta 390, Barcelona 08017, Spain.
Antoni PlanasLaboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull, Via Augusta 390, Barcelona 08017, Spain.
Tom DesmetCentre for Synthetic Biology (CSB), Department of Biotechnology, Ghent University, Coupure Links 653, Ghent 9000, Belgium.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

UDP-galactose 4-epimerases (Gal4Es) catalyze the inversion of the 4-hydroxyl configuration of a sugar moiety from an NDP-sugar through a three-step process: oxidation, rotation and reduction. Despite extensive biochemical and structural studies, the role of protein dynamics on substrate specificity remains poorly understood. The recently identified subgroup of GDP-sugar 4-epimerases, notable for its exceptional substrate promiscuity, provides an intriguing model to investigate the role of dynamics in the Gal4E catalytic mechanism and the unique promiscuity of the subgroup. In this study, we used a multidisciplinary approach to examine the dynamic-function relationships in the

Indexed as

Carbohydrate epimerases (CEP1)GDP-sugar 4-epimeraseHeptagonal box modelL-sugarsMolecular dynamics simulationsNucleotide-sugarsSugar ring rotationUDP-galactose 4-epimerase

Identifiers

PMID40529184
PMCPMC12171764

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.