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- W4387642016 abstract "Orchestrated action of peptidoglycan (PG) synthetases and hydrolases is vital for bacterial growth and viability. Although the function of several PG synthetases e.g., penicillin binding proteins is well-understood, the function, regulation, and mechanism of action of the majority of PG hydrolases have remained elusive. Lysostaphin-like zinc-dependent metalloendopeptidases specifically hydrolyse the glycyl-glycine peptide bond in the notorious pathogen Staphylococcus aureus. In this work, we have employed NMR spectroscopy to study the substrate specificity of the well-established bactericide lysostaphin as well as pre-designated S. aureus autolysin LytM. Our results show that the substrate specificities of these highly homologous enzymes are divergent and formerly also inaccurately defined. Yet, we provide substrate-level evidence for the functional role of these enzymes. Indeed, we show that LytM and anti-staphylococcal bactericidin lysostaphin target the D-Ala-Gly cross-linked part of mature peptidoglycan." @default.
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- W4387642016 date "2023-10-13" @default.
- W4387642016 modified "2023-10-15" @default.
- W4387642016 title "Reassessing the substrate specificities of the major Staphylococcus aureus peptidoglycan hydrolases lysostaphin and LytM" @default.
- W4387642016 doi "https://doi.org/10.1101/2023.10.13.562287" @default.
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