Reassessing the substrate specificities of the major Staphylococcus aureus peptidoglycan hydrolases lysostaphin and LytM (Updated August 2, 2024).

This article discusses a study that aims to understand the substrate specificities of two major peptidoglycan hydrolases, lysostaphin and LytM, in Staphylococcus aureus bacteria. The researchers used NMR spectroscopy to investigate the substrate specificity and bond cleavage of these enzymes. The results show that both lysostaphin and LytM prefer the D-Ala-Gly cross-linked part of mature peptidoglycan, but LytM can also act as a D-alanyl-glycine endopeptidase. This research provides valuable insights into the function and regulation of these enzymes. [Extracted from the article]