ReviewMicrobiology and molecular biology reviews : MMBR2011
Peptidoglycan hydrolases of Escherichia coli.
Review in Microbiology and molecular biology reviews : MMBR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.
What it found
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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.
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Who cites it
128 citing papers in PubMed, 225 citations in OpenAlex.
- Article
- Using Single-Particle Fluorescence Microscopy to Quantify Substrate Binding of Peptidoglycan-Modification Enzymes.Bio-protocol · 2026Article
- Peptidoglycan recycling is critical for cell division, cell wall integrity, and β-lactam resistance ineLife · 2026Article
- Novel Ternary Biopolymer Films Incorporating Amygdalin: FTIR, TG, and In Vitro Evaluation on Model Bacteria.Materials (Basel, Switzerland) · 2026Article
- Enzymatic activity of PBP1B is required for growth rate-independent ppGpp-mediated resistance to PBP2 inhibitors inJournal of bacteriology · 2026Article
- Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025Review
- Milestones in the development ofJournal of bacteriology · 2025Review
- A novel mechanism for bacterial sporulation based on programmed peptidoglycan degradation.bioRxiv : the preprint server for biology · 2025Article
- Third track model for coordination of septal peptidoglycan synthesis and degradation by FtsN in Escherichia coli.Nature microbiology · 2025Article
- Article
- Isolation and characterization of a novel lytic bacteriophage Pv27 with biocontrol potential againstPeerJ · 2025Article
- Editorial: Reviews in microbial pathogenesis.Frontiers in microbiology · 2025Article
- Identification of Potential Inhibitors ofACS omega · 2024Article
- Peptidoglycan Endopeptidase PBP7 Facilitates the Recruitment of FtsN to the Divisome and Promotes Peptidoglycan Synthesis in Escherichia coli.Molecular microbiology · 2024Article
- Lactic acid bacteria secreted proteins as potential Listeria monocytogenes quorum sensing inhibitors.Molecular diversity · 2024Article
- A lytic transglycosylase connects bacterial focal adhesion complexes to the peptidoglycan cell wall.eLife · 2024Article
- A lytic transglycosylase connects bacterial focal adhesion complexes to the peptidoglycan cell wall.bioRxiv : the preprint server for biology · 2024Article
- TargetingAntibiotics (Basel, Switzerland) · 2024Article
- Structural basis for recruitment of peptidoglycan endopeptidase MepS by lipoprotein NlpI.Nature communications · 2024Article
- P. aeruginosa CtpA protease adopts a novel activation mechanism to initiate the proteolytic process.The EMBO journal · 2024Article
68 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The review summarizes the abundant information on the 35 identified peptidoglycan (PG) hydrolases of Escherichia coli classified into 12 distinct families, including mainly glycosidases, peptidases, and amidases. An attempt is also made to critically assess their functions in PG maturation, turnover, elongation, septation, and recycling as well as in cell autolysis. There is at least one hydrolytic activity for each bond linking PG components, and most hydrolase genes were identified. Few hydrolases appear to be individually essential. The crystal structures and reaction mechanisms of certain hydrolases having defined functions were investigated. However, our knowledge of the biochemical properties of most hydrolases still remains fragmentary, and that of their cellular functions remains elusive. Owing to redundancy, PG hydrolases far outnumber the enzymes of PG biosynthesis. The presence of the two sets of enzymes acting on the PG bonds raises the question of their functional correlations. It is difficult to understand why E. coli keeps such a large set of PG hydrolases. The subtle differences in substrate specificities between the isoenzymes of each family certainly reflect a variety of as-yet-unidentified physiological functions. Their study will be a far more difficult challenge than that of the steps of the PG biosynthesis pathway.
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What OpenQuestion holds
Registered trials
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.