ArticleScientific reports2022
Diversity of the lysozyme fold: structure of the catalytic domain from an unusual endolysin encoded by phage Enc34.
Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 19 citations in OpenAlex.
- Structure of NO16, a marine non-tailed vibriophage with an unusual symmetry-mismatched vertex arrangement.PLoS pathogens · 2026Article
- Genomic characterization of Pseudomonas aeruginosa clonal lineage ST162 isolated from bovine-milk in South Africa.BMC microbiology · 2026Article
- Investigation of Recombinantly Produced Endolysins Reveals a Modular Enzyme Shared by Several Enterobacteria Phages to Exhibit Broad-Range Lytic Activity Against Different Orders of Gammaproteobacteria.MicrobiologyOpen · 2026Article
- Exploring the Antimicrobial Potential of a Novel Phage-Derived Lytic Protein AgainstCurrent issues in molecular biology · 2026Article
- In silico exploration of the genomic repertoire of Iranian aquatic bacteria: Prophage carriage, bioactive compound potential, CRISPR-Cas immunity, and integrated defensive-metabolic islands.Biochemistry and biophysics reports · 2026Article
- Metagenomic and physicochemical profiling reveal microbial functions in pit mud for Jiang-Nong Jianxiang Baijiu fermentation.BMC microbiology · 2025Article
- Molecular Docking of Endolysins for Studying Peptidoglycan Binding Mechanism.Molecules (Basel, Switzerland) · 2024Article
- Origin, Evolution and Diversity of φ29-like Phages-Review and Bioinformatic Analysis.International journal of molecular sciences · 2024Review
- Xanthomonas immunity proteins protect against the cis-toxic effects of their cognate T4SS effectors.EMBO reports · 2024Article
- Recombinant design of the enzymatically active domain of phage Enc34 endolysin to improve its activity against Gram-negative bacteria.FEMS microbiology letters · 2024Article
- Molecular Machinery of the Triad Holin, Endolysin, and Spanin: Key Players Orchestrating Bacteriophage-Induced Cell Lysis and their Therapeutic Applications.Protein and peptide letters · 2024Review
- Recent advances in therapeutic targets identification and development of treatment strategies towards Pseudomonas aeruginosa infections.BMC microbiology · 2023Review
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endolysins are bacteriophage-encoded peptidoglycan-degrading enzymes with potential applications for treatment of multidrug-resistant bacterial infections. Hafnia phage Enc34 encodes an unusual endolysin with an N-terminal enzymatically active domain and a C-terminal transmembrane domain. The catalytic domain of the endolysin belongs to the conserved protein family PHA02564 which has no recognizable sequence similarity to other known endolysin types. Turbidity reduction assays indicate that the Enc34 enzyme is active against peptidoglycan from a variety of Gram-negative bacteria including the opportunistic pathogen Pseudomonas aeruginosa PAO1. The crystal structure of the catalytic domain of the Enc34 endolysin shows a distinctive all-helical architecture that distantly resembles the α-lobe of the lysozyme fold. Conserved catalytically important residues suggest a shared evolutionary history between the Enc34 endolysin and GH73 and GH23 family glycoside hydrolases and propose a molecular signature for substrate cleavage for a large group of peptidoglycan-degrading enzymes.
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