Structural and functional studies on lysostaphin, an antistaphylococcal endopeptidase
Rochette, Sophie (2009) Structural and functional studies on lysostaphin, an antistaphylococcal endopeptidase. PhD thesis, University of Nottingham.
This PhD thesis describes research into the structure and function of lysostaphin (EC 188.8.131.52), a glycylglycine endopeptidase secreted by Staphylococcus simulans biovar staphylolyticus ATCC 1362. Lysostaphin is a member of the M23/M37 zinc metalloprotease family and is a pre-pro-enzyme. The mature form (after removal of the pro-region) contains two distinct domains, the C-terminal cell wall targeting domain of lysostaphin (termed LssTdom in the thesis) facilitates binding to Staphylococcus aureus cells. The endopeptidase domain (termed LssEdom in the thesis) cleaves the pentaglycine crosslinks in the peptidoglycan resulting in cell death through cell rupture of S. aureus.
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