Evidence map›Paper›PMID 25277548›Full record

ArticleBiochimica et biophysica acta2015

Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis.

Matías D Asención Diez, Ana M Demonte, Karl Syson, Diego G Arias, Andrii Gorelik, Sergio A Guerrero, Stephen Bornemann, Alberto A Iglesias

Open access · hybridAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Immobilization of the Highly Active UDP-Glucose Pyrophosphorylase FromFrontiers in bioengineering and biotechnology · 2020
    Article
  4. Article
  5. Two Homologous Enzymes of the GalU Family inInternational journal of molecular sciences · 2019
    Article
  6. TheThe Biochemical journal · 2019
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Distribution of glucan-branching enzymes among prokaryotes.Cellular and molecular life sciences : CMLS · 2016
    Review
  12. Article
  13. Article
  14. Review
  15. 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

8 authors at 3 institutions in 2 countries.

Matías D Asención DiezInstituto de Agrobiotecnología del Litoral (UNL-CONICET), Facultad de Bioquímica y Ciencias Biológicas, Paraje El Pozo, S3000ZAA Santa Fe, Argentina.
Ana M DemonteInstituto de Agrobiotecnología del Litoral (UNL-CONICET), Facultad de Bioquímica y Ciencias Biológicas, Paraje El Pozo, S3000ZAA Santa Fe, Argentina.
Karl SysonDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Diego G AriasInstituto de Agrobiotecnología del Litoral (UNL-CONICET), Facultad de Bioquímica y Ciencias Biológicas, Paraje El Pozo, S3000ZAA Santa Fe, Argentina.
Andrii GorelikDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Sergio A GuerreroInstituto de Agrobiotecnología del Litoral (UNL-CONICET), Facultad de Bioquímica y Ciencias Biológicas, Paraje El Pozo, S3000ZAA Santa Fe, Argentina.
Stephen BornemannDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Alberto A IglesiasInstituto de Agrobiotecnología del Litoral (UNL-CONICET), Facultad de Bioquímica y Ciencias Biológicas, Paraje El Pozo, S3000ZAA Santa Fe, Argentina. Electronic address: iglesias@fbcb.unl.edu.ar.
Instituto de Agrobiotecnología del Litoral · ARJohn Innes Centre · GBNorwich Research Park · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/E/J/000C0647
6 · The paper itself

Abstract

backgroundMycobacterium tuberculosis is a pathogenic prokaryote adapted to survive in hostile environments. In this organism and other Gram-positive actinobacteria, the metabolic pathways of glycogen and trehalose are interconnected.

resultsIn this work we show the production, purification and characterization of recombinant enzymes involved in the partitioning of glucose-1-phosphate between glycogen and trehalose in M. tuberculosis H37Rv, namely: ADP-glucose pyrophosphorylase, glycogen synthase, UDP-glucose pyrophosphorylase and trehalose-6-phosphate synthase. The substrate specificity, kinetic parameters and allosteric regulation of each enzyme were determined. ADP-glucose pyrophosphorylase was highly specific for ADP-glucose while trehalose-6-phosphate synthase used not only ADP-glucose but also UDP-glucose, albeit to a lesser extent. ADP-glucose pyrophosphorylase was allosterically activated primarily by phosphoenolpyruvate and glucose-6-phosphate, while the activity of trehalose-6-phosphate synthase was increased up to 2-fold by fructose-6-phosphate. None of the other two enzymes tested exhibited allosteric regulation.

conclusionsResults give information about how the glucose-1-phosphate/ADP-glucose node is controlled after kinetic and regulatory properties of key enzymes for mycobacteria metabolism. GENERAL SIGNIFICANCE: This work increases our understanding of oligo and polysaccharides metabolism in M. tuberculosis and reinforces the importance of the interconnection between glycogen and trehalose biosynthesis in this human pathogen.

Indexed as

Metabolic Networks and PathwaysAllosteric RegulationBacterial ProteinsGlucose-1-Phosphate AdenylyltransferaseGlucose-6-PhosphateGlucosephosphatesGlucosyltransferasesGlycogenGlycogen SynthaseKineticsModels, BiologicalMycobacterium tuberculosisRecombinant ProteinsSubstrate SpecificityTrehaloseUTP-Glucose-1-Phosphate UridylyltransferaseBacterial Proteinsglucose-1-phosphateGlucose-1-Phosphate AdenylyltransferaseGlucose-6-PhosphateGlucosephosphatesGlucosyltransferasesGlycogenGlycogen SynthaseRecombinant ProteinsTrehalosetrehalose-6-phosphate synthaseUTP-Glucose-1-Phosphate UridylyltransferaseADP-glucose pyrophosphorylaseGlucose-6-phosphateGlycogen synthasePhosphoenolpyruvateTrehalose-6-phosphate synthaseUDP-glucose pyrophosphorylase

Identifiers

PMID25277548
PMCPMC4331664
OpenAlexW2040544293

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.