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  • Inhibition of the activity of both domains of lysostaphin through peptidoglycan modification by the lysostaphin immunity protein.

Inhibition of the activity of both domains of lysostaphin through peptidoglycan modification by the lysostaphin immunity protein.

Applied and environmental microbiology (2010-08-24)
Shaw R Gargis, Harry E Heath, Paul A LeBlanc, Linda Dekker, Robin S Simmonds, Gary L Sloan
RESUMEN

Resistance to lysostaphin, a staphylolytic glycylglycine endopeptidase, is due to a FemABX-like immunity protein that inserts serines in place of some glycines in peptidoglycan cross bridges. These modifications inhibit both binding of the recombinant cell wall targeting domain and catalysis by the recombinant catalytic domain of lysostaphin.

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Sigma-Aldrich
Lisostafina from Staphylococcus staphylolyticus, lyophilized powder, Protein 50-70 % by biuret, ≥500 units/mg protein
Sigma-Aldrich
Lysostaphin from Staphylococcus simulans, recombinant, expressed in E. coli, lyophilized powder
Sigma-Aldrich
Lisostafina from Staphylococcus staphylolyticus, BioUltra, ≥97% (SDS-PAGE), Protein 40-60 % by biuret, ≥2,000 units/mg protein
Sigma-Aldrich
Lisostafina from Staphylococcus staphylolyticus, aseptically filled