0000000001170086

AUTHOR

Vesa P. Kontinen

showing 1 related works from this author

Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family

2017

AbstractWe 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 …

0301 basic medicineentsyymitantimicrobial compoundsPROTEINchemistry.chemical_compoundCatalytic DomainCELL-WALLBINDINGMultidisciplinaryACTIVE-SITEQRESISTANT STAPHYLOCOCCUS-AUREUSRHydrogen-Ion ConcentrationAnti-Bacterial AgentsZincBiochemistryMedicineHISTIDINESProtein BindingStaphylococcus aureusScienceenzymesBiologyCleavage (embryo)metalloproteinasesArticleCofactorBACILLUS-SUBTILISCell wallStructure-Activity Relationship03 medical and health sciencesEndopeptidasesProtein Interaction Domains and MotifsAmino Acid Sequencestaphylococciantimikrobiset yhdisteetBinding SitesLysostaphinCell MembraneActive siteIsothermal titration calorimetryPeriplasmic spaceVANCOMYCINstafylokokitmetalloproteinaasitMODEL030104 developmental biologyRESOLUTIONchemistryMutationProteolysisLysostaphinbiology.protein1182 Biochemistry cell and molecular biologyPeptidoglycanScientific Reports
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