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Merck

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
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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.

MATERIALS
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Sigma-Aldrich
Lysostaphin from Staphylococcus simulans, recombinant, expressed in E. coli, lyophilized powder
Sigma-Aldrich
Lysostaphin from Staphylococcus staphylolyticus, BioUltra, โ‰ฅ97% (SDS-PAGE), Protein 40-60 % by biuret, โ‰ฅ2,000 units/mg protein