Staphylococcus aureus substrates

Amikadn Phosphorylation 3 -0-Phosphorylated Staphylococcus aureus derivatives of the respective substrates ... 

Neamine Neomydn Ribostamydn Gentamicins A, B, Cia. c2 Kanamydn B Sisomidn Tobramydn Dihydrostreptomydn Pseudomonas aeruginosa Escherichia coli Pseudomonas aeruginosa Escherichia coli Staphylococcus aureus 3 -0-Phosphorylated Pseudomonas aeruginosa derivatives of the respective substrates ... 

Several types of testing were employed to evaluate the bactericidal efficacies of the coated substrates. Five of the coatings on circular glass cover-slips (12 mm diameter) were challenged with the bacterium Staphylococcus aureus (ATCC 6538). This was accomplished by adding a 50- jlL suspension of 10 CFU S. aureus to the surface of each sample. At predetermined contact times a 25- jlL aliquot was removed from the surface, quenched with sterile 0.02 N sodium thiosulfate, and plated on nutrient agar. The viable bacterial colonies were then counted after 48 h incubation at 37°C. Fabric samples were tested by two methods. In one, small squares (1.0-1.5 cm) were placed on a Tryptic Soy agar plate that was inoculated... 

Tincture of the dried seed, on agar plate at a concentration of 30 p,L/disc, was inactive on Escherichia coli, Pseudomonas aeruginosa, and Staphylococcus aureus. Extract of 10 g plant material in 100 mL ethanol was used b Anticoagulation activity. Serpin BSZx (an inhibitor of trypsin and chemotrypsin) inhibited thrombin, plasma kallikrein, factor Vlla/tissue factor, and factor Xa at heparin-independent association rates. Only factor Xa turned a significant fraction of BSZx over as substrate. Activated protein C and leukocyte elastase were slowly inhibited by BSZx, whereas factor Xlla, urokinase and tissue type plasminogen activator, plasmin and pancreas kallikrein, and elastase were not or only weakly affected. Trypsin from Fusarium was not inhibited, while interaction with subtilisin Carlsberg and Novo was rapid, but most BSZx was cleaved as a substrate L... 

Staphylococcus aureus V8 protease deaves proteins specifically after glutamate residues, provided that the following residue is not proline, or a further glutamate or aspartate. In ammonium bicarbonate buffer at pH 7.8, the enzyme is very specific for glutamate in Na-phosphate buffer at the same pH it also cleaves adjacent to aspartate. V8 protease is added at a ratio of 1-2% (w/w) to the protein substrate. Reaction can be stopped by freezing, or by the addition of PMSF or a2-rtiacroglobu-lin. 

Paulsen IT, Brown MH, Littlejohn TG, Mitchell BA, Skurray RA. Multidrug resistance proteins QacA and QacB from Staphylococcus aureus membrane topology and identification of residues involved in substrate specificity. Proc. Natl. Acad. Sci. U.S.A. 1996 93 3630-3635. 

Standard mechanism inhibitors are classified strictly as inhibitors of serine proteases. There have been reports of inhibitors of other classes of proteases that have similar mechanisms to those of standard mechanism inhibitors, though. Initial studies on the streptomyces metalloprotease inhibitor (SMPl) suggest that it inhibits the metalloprotease thermolysin through a substrate-like binding mechanism (2). Similarly, staphostatin B, a cysteine protease inhibitor from Staphylococcus aureus, binds in a substrate-like manner in the active site of staphopain cysteine proteases. However, staphostatin B has a glycine PI residue, which adopts a backbone conformation that seems to prevent nucleophilic attack of the scissiie bond (3). 

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