Evidence map›Paper›PMID 31681755›Full record

ArticleFrontiers in bioengineering and biotechnology2019

Enhancing PLP-Binding Capacity of Class-III ω-Transaminase by Single Residue Substitution.

David Roura Padrosa, Raphael Alaux, Phillip Smith, Ingrid Dreveny, Fernando López-Gallego, Francesca Paradisi

Abstract read
In one paragraph

Article in Frontiers in bioengineering and biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Crystal structure of the plant GABA aminotransferase AtGABA-T from Arabidopsis thaliana.Acta crystallographica. Section F, Structural biology communications · 2026
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  9. Biocatalytic cascade to polysaccharide amination.Biotechnology for biofuels and bioproducts · 2024
    Article
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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.

David Roura PadrosaSchool of Chemistry, University of Nottingham, Nottingham, United Kingdom.
Raphael AlauxSchool of Chemistry, University of Nottingham, Nottingham, United Kingdom.
Phillip SmithCentre for Biomolecular Sciences, University of Nottingham, Nottingham, United Kingdom.
Ingrid DrevenyCentre for Biomolecular Sciences, University of Nottingham, Nottingham, United Kingdom.
Fernando López-GallegoInstituto de Síntesis Química y Catálisis Homogénea, Zaragoza, Spain.
Francesca ParadisiSchool of Chemistry, University of Nottingham, Nottingham, United Kingdom.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transaminases are pyridoxal-5'-phosphate (PLP) binding enzymes, broadly studied for their potential industrial application. Their affinity for PLP has been related to their performance and operational stability and while significant differences in PLP requirements have been reported, the environment of the PLP-binding pocket is highly conserved. In this study, thorough analysis of the residue interaction network of three homologous transaminases

Indexed as

biocatalysisprotein engineeringprotein stabilitypyridoxal phosphatetransaminase

Identifiers

PMID31681755
PMCPMC6813460

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.