ArticleScientific reports2017
Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Characterization of VldE (Spr1875), a Pneumococcal Two-State l,d-Endopeptidase with a Four-Zinc Cluster in the Active Site.ACS catalysis · 2024Article
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- Agents Targeting the Bacterial Cell Wall as Tools to Combat Gram-Positive Pathogens.Molecules (Basel, Switzerland) · 2024Review
- Chemical shift assignments of the catalytic domain of Staphylococcus aureus LytM.Biomolecular NMR assignments · 2024Article
- Identification of a putative cell wall-hydrolyzing amidase involved in sporangiospore maturation inJournal of bacteriology · 2024Article
- Article
- Structural and Functional Characterization of β-lytic Protease fromInternational journal of molecular sciences · 2022Article
- Staphylococcus aureus cell wall maintenance - the multifaceted roles of peptidoglycan hydrolases in bacterial growth, fitness, and virulence.FEMS microbiology reviews · 2022Review
- Electrostatic Interaction with the Bacterial Cell Envelope Tunes the Lytic Activity of Two Novel Peptidoglycan Hydrolases.Microbiology spectrum · 2022Article
- One fold, many functions-M23 family of peptidoglycan hydrolases.Frontiers in microbiology · 2022Review
- Diversity of bacteriocins in the microbiome of the Tucuruí Hydroelectric Power Plant water reservoir and three-dimensional structure prediction of a zoocin.Genetics and molecular biology · 2022Article
- Differential binding of human and murine IgGs to catalytic and cell wall binding domains of Staphylococcus aureus peptidoglycan hydrolases.Scientific reports · 2021Article
- Structural Characterization of EnpA D,L-Endopeptidase fromInternational journal of molecular sciences · 2021Article
- Article
- Two New M23 Peptidoglycan Hydrolases With Distinct Net Charge.Frontiers in microbiology · 2021Article
- Enzyme-Functionalized Mesoporous Silica Nanoparticles to TargetInternational journal of nanomedicine · 2021Article
- A Simple Protocol for the Determination of Lysostaphin Enzymatic Activity.Antibiotics (Basel, Switzerland) · 2020Article
- LytU-SH3b fusion protein as a novel and efficient enzybiotic against methicillin-resistantMolecular biology research communications · 2019Article
- Interaction of host and Staphylococcus aureus protease-system regulates virulence and pathogenicity.Medical microbiology and immunology · 2019Review
- Structural and Functional Insights Into Lysostaphin-Substrate Interaction.Frontiers in molecular biosciences · 2018Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We introduce LytU, a short member of the lysostaphin family of zinc-dependent pentaglycine endopeptidases. It is a potential antimicrobial agent for S. aureus infections and its gene transcription is highly upregulated upon antibiotic treatments along with other genes involved in cell wall synthesis. We found this enzyme to be responsible for the opening of the cell wall peptidoglycan layer during cell divisions in S. aureus. LytU is anchored in the plasma membrane with the active part residing in the periplasmic space. It has a unique Ile/Lys insertion at position 151 that resides in the catalytic site-neighbouring loop and is vital for the enzymatic activity but not affecting the overall structure common to the lysostaphin family. Purified LytU lyses S. aureus cells and cleaves pentaglycine, a reaction conveniently monitored by NMR spectroscopy. Substituting the cofactor zinc ion with a copper or cobalt ion remarkably increases the rate of pentaglycine cleavage. NMR and isothermal titration calorimetry further reveal that, uniquely for its family, LytU is able to bind a second zinc ion which is coordinated by catalytic histidines and is therefore inhibitory. The pH-dependence and high affinity of binding carry further physiological implications.
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