Evidence map›Paper›PMID 26370943›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2015

Activities and regulation of peptidoglycan synthases.

Alexander J F Egan, Jacob Biboy, Inge van't Veer, Eefjan Breukink, Waldemar Vollmer

Open access · bronzeAbstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
11.5field-weighted citation impact, top 1% 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

93 citing papers in PubMed, 176 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. ThemBio · 2026
    Article
  5. Article
  6. Peptidoglycan LD-Transpeptidases.Antibiotics (Basel, Switzerland) · 2025
    Review
  7. Lipid II unlocked: strategies for obtaining a major antibiotic target.Chemical communications (Cambridge, England) · 2025
    Review
  8. Article
  9. International journal of systematic and evolutionary microbiology · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. A bifunctionalOrganic & biomolecular chemistry · 2024
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

33 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Alexander J F EganCentre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Richardson Road, Newcastle upon Tyne NE2 4AX, UK.
Jacob BiboyCentre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Richardson Road, Newcastle upon Tyne NE2 4AX, UK.
Inge van't VeerMembrane Biochemistry and Biophysics, Bijvoet Centre for Biomolecular Research, University of Utrecht, Padualaan 8, 3584 Utrecht, The Netherlands.
Eefjan BreukinkMembrane Biochemistry and Biophysics, Bijvoet Centre for Biomolecular Research, University of Utrecht, Padualaan 8, 3584 Utrecht, The Netherlands.
Waldemar VollmerCentre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Richardson Road, Newcastle upon Tyne NE2 4AX, UK w.vollmer@ncl.ac.uk.
Newcastle University · GBUtrecht University · NL

Funding

Wellcome Trust 101824Wellcome Trust 101824/Z/13/Z
6 · The paper itself

Abstract

Peptidoglycan (PG) is an essential component in the cell wall of nearly all bacteria, forming a continuous, mesh-like structure, called the sacculus, around the cytoplasmic membrane to protect the cell from bursting by its turgor. Although PG synthases, the penicillin-binding proteins (PBPs), have been studied for 70 years, useful in vitro assays for measuring their activities were established only recently, and these provided the first insights into the regulation of these enzymes. Here, we review the current knowledge on the glycosyltransferase and transpeptidase activities of PG synthases. We provide new data showing that the bifunctional PBP1A and PBP1B from Escherichia coli are active upon reconstitution into the membrane environment of proteoliposomes, and that these enzymes also exhibit DD-carboxypeptidase activity in certain conditions. Both novel features are relevant for their functioning within the cell. We also review recent data on the impact of protein-protein interactions and other factors on the activities of PBPs. As an example, we demonstrate a synergistic effect of multiple protein-protein interactions on the glycosyltransferase activity of PBP1B, by its cognate lipoprotein activator LpoB and the essential cell division protein FtsN.

Indexed as

Escherichia coliEscherichia coli ProteinsKineticsModels, MolecularPenicillin-Binding ProteinsPeptidoglycanPeptidoglycan GlycosyltransferaseSubstrate SpecificityEscherichia coli ProteinsPenicillin-Binding ProteinsPeptidoglycanPeptidoglycan Glycosyltransferasecarboxypeptidaseglycosyltransferaselipid IIpenicillin-binding proteinpeptidoglycantranspeptidase

Identifiers

PMID26370943
PMCPMC4632607
OpenAlexW1478816797

What OpenQuestion holds

Textmetadata
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.