Evidence map›Paper›PMID 20048065›Full record

ArticleApplied and environmental microbiology2010

Lactobacillus reuteri 2'-deoxyribosyltransferase, a novel biocatalyst for tailoring of nucleosides.

Jesús Fernández-Lucas, Carmen Acebal, José V Sinisterra, Miguel Arroyo, Isabel de la Mata

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2010. 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
1.2field-weighted citation impact, top 22% of its field
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, 49 citations in OpenAlex.

  1. Article
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  5. Article
  6. A Multi-enzyme Cascade for the Biosynthesis of AICA Ribonucleoside Di- and Triphosphate.Chembiochem : a European journal of chemical biology · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Hypoxanthine-Guanine Phosphoribosyltransferase/adenylate Kinase FromFrontiers in bioengineering and biotechnology · 2020
    Article
  12. Frontiers in bioengineering and biotechnology · 2020
    Article
  13. Article
  14. 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

5 authors at 1 institution in 1 country.

Jesús Fernández-LucasDepartment of Biochemistry and Molecular Biology I, Faculty of Biology, Complutense University of Madrid, C/ José Antonio Nováis 2, 28040 Madrid, Spain.
Carmen Acebal
José V Sinisterra
Miguel Arroyo
Isabel de la Mata
Universidad Complutense de Madrid · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A novel type II nucleoside 2'-deoxyribosyltransferase from Lactobacillus reuteri (LrNDT) has been cloned and overexpressed in Escherichia coli. The recombinant LrNDT has been structural and functionally characterized. Sedimentation equilibrium analysis revealed a homohexameric molecule of 114 kDa. Circular dichroism studies have showed a secondary structure containing 55% alpha-helix, 10% beta-strand, 16% beta-sheet, and 19% random coil. LrNDT was thermostable with a melting temperature (T(m)) of 64 degrees C determined by fluorescence, circular dichroism, and differential scanning calorimetric studies. The enzyme showed high activity in a broad pH range (4.6 to 7.9) and was also very stable between pH 4 and 7.9. The optimal temperature for activity was 40 degrees C. The recombinant LrNDT was able to synthesize natural and nonnatural nucleoside analogues, improving activities described in the literature, and remarkably, exhibited unexpected new arabinosyltransferase activity, which had not been described so far in this kind of enzyme. Furthermore, synthesis of new arabinonucleosides and 2'-fluorodeoxyribonucleosides was carried out.

Indexed as

Bacterial ProteinsCircular DichroismCloning, MolecularEnzymesEnzyme StabilityEscherichia coliGene ExpressionHot TemperatureHydrogen-Ion ConcentrationKineticsLimosilactobacillus reuteriMolecular WeightNucleosidesPentosyltransferasesProtein MultimerizationProtein Structure, SecondaryarabinosyltransferaseBacterial ProteinsEnzymesnucleoside deoxyribosyltransferase IINucleosidesPentosyltransferases

Identifiers

PMID20048065
PMCPMC2832402
OpenAlexW2053263061

What OpenQuestion holds

Textmetadata
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.