Evidence map›Paper›PMID 31330931›Full record

ArticleInternational journal of molecular sciences2019

Characterization of the First Bacterial and Thermostable GDP-Mannose 3,5-Epimerase.

Ophelia Gevaert, Stevie Van Overtveldt, Koen Beerens, Tom Desmet

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
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

4 authors.

Ophelia GevaertCentre for Synthetic Biology, Department of Biotechnology, Ghent University, Coupure links 653, 9000 Gent, Belgium.
Stevie Van OvertveldtCentre for Synthetic Biology, Department of Biotechnology, Ghent University, Coupure links 653, 9000 Gent, Belgium.
Koen BeerensCentre for Synthetic Biology, Department of Biotechnology, Ghent University, Coupure links 653, 9000 Gent, Belgium.
Tom DesmetCentre for Synthetic Biology, Department of Biotechnology, Ghent University, Coupure links 653, 9000 Gent, Belgium. tom.desmet@ugent.be.ORCID 0000-0002-5788-3022

Funding

Fonds Wetenschappelijk Onderzoek 1S16817NFonds Wetenschappelijk Onderzoek G0F3417N
6 · The paper itself

Abstract

GDP-mannose 3,5-epimerase (GM35E) catalyzes the conversion of GDP-mannose towards GDP-l-galactose and GDP-l-gulose. Although this reaction represents one of the few enzymatic routes towards the production of l-sugars and derivatives, it has not yet been exploited for that purpose. One of the reasons is that so far only GM35Es from plants have been characterized, yielding biocatalysts that are relatively unstable and difficult to express heterologously. Through the mining of sequence databases, we succeeded in identifying a promising bacterial homologue. The gene from the thermophilic organism

Indexed as

Bacterial ProteinsAmino Acid SequenceCarbohydrate EpimerasesCatalysisEnzyme ActivationEnzyme StabilityGuanosine Diphosphate MannoseHydrogen-Ion ConcentrationModels, MolecularMolecular StructureProtein ConformationRecombinant ProteinsStructure-Activity RelationshipThermodynamicsBacterial ProteinsCarbohydrate EpimerasesGDPmannose 3,5-epimeraseGuanosine Diphosphate MannoseRecombinant ProteinsbiocatalysisGDP-mannose 3,5-epimerasel-sugarsMethylacidiphilum fumariolicumrecombinant expression

Identifiers

PMID31330931
PMCPMC6678494

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.