Evidence map›Paper›PMID 23555903›Full record

ArticlePloS one2013

Characterisation of ATP-dependent Mur ligases involved in the biogenesis of cell wall peptidoglycan in Mycobacterium tuberculosis.

Tulika Munshi, Antima Gupta, Dimitrios Evangelopoulos, Juan David Guzman, Simon Gibbons, Nicholas H Keep, Sanjib Bhakta

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

43 citing papers in PubMed, 87 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Age-Dependent Pleomorphism inMicroorganisms · 2025
    Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Prospects for Antibacterial Discovery and Development.Journal of the American Chemical Society · 2021
    Article
  12. Journal of enzyme inhibition and medicinal chemistry · 2021
    Article
  13. Article
  14. Characterization of the MurT/GatD complex inJAC-antimicrobial resistance · 2021
    Article
  15. Review
  16. iScience · 2020
    Article
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Tulika MunshiDepartment of Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck, University of London, London, United Kingdom.
Antima Gupta
Dimitrios Evangelopoulos
Juan David Guzman
Simon Gibbons
Nicholas H Keep
Sanjib Bhakta
Institute of Structural and Molecular Biology · GBBirkbeck, University of London · GBUniversity College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F011148/1Medical Research Council G0801956Medical Research Council G0802079
6 · The paper itself

Abstract

ATP-dependent Mur ligases (Mur synthetases) play essential roles in the biosynthesis of cell wall peptidoglycan (PG) as they catalyze the ligation of key amino acid residues to the stem peptide at the expense of ATP hydrolysis, thus representing potential targets for antibacterial drug discovery. In this study we characterized the division/cell wall (dcw) operon and identified a promoter driving the co-transcription of mur synthetases along with key cell division genes such as ftsQ and ftsW. Furthermore, we have extended our previous investigations of MurE to MurC, MurD and MurF synthetases from Mycobacterium tuberculosis. Functional analyses of the pure recombinant enzymes revealed that the presence of divalent cations is an absolute requirement for their activities. We also observed that higher concentrations of ATP and UDP-sugar substrates were inhibitory for the activities of all Mur synthetases suggesting stringent control of the cytoplasmic steps of the peptidoglycan biosynthetic pathway. In line with the previous findings on the regulation of mycobacterial MurD and corynebacterial MurC synthetases via phosphorylation, we found that all of the Mur synthetases interacted with the Ser/Thr protein kinases, PknA and PknB. In addition, we critically analyzed the interaction network of all of the Mur synthetases with proteins involved in cell division and cell wall PG biosynthesis to re-evaluate the importance of these key enzymes as novel therapeutic targets in anti-tubercular drug discovery.

Indexed as

Adenosine TriphosphateBacterial ProteinsCell WallChromatography, High Pressure LiquidMycobacterium tuberculosisPeptide SynthasesPeptidoglycanPhosphorylationProtein BindingProtein FoldingProtein Serine-Threonine KinasesAdenosine TriphosphateBacterial ProteinsMurE protein, Mycobacterium tuberculosisPeptide SynthasesPeptidoglycanPknA protein, Mycobacterium tuberculosisPknB protein, Mycobacterium tuberculosisProtein Serine-Threonine KinasesUDP-N-acetylmuramoylalanine-D-glutamate ligase

Identifiers

PMID23555903
PMCPMC3605390
OpenAlexW2089091853

What OpenQuestion holds

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LicenceCC BY
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.