Methods

In Vitro Activities of a Novel Cephalosporin, CB-181963 (CAB-175), against Methicillin-Susceptible or -Resistant Staphylococcus aureus and Glycopeptide-Intermediate Susceptible Staphylococci.
Vanthida Huang, 2004.We examined the activity of CB-181963, a novel cephalosporin, against methicillin-resistant Staphylococcus aureus (MRSA) (n = 200), methicillin-susceptible S . aureus (MSSA) (n = 50), glycopeptide-intermediate Staphylococcus species (GISS) (n = 47), and VRSA (n = 2) isolates . CB-181963 exhibited MIC profiles similar to those of linezolid against MRSA and GISS; however, activity against MSSA was similar to that of vancomycin . Time-kill study results of investigations of activity against MRSA, MSSA, and GISS at 24 h were as follows: CB-181963 activity = vancomycin activity > linezolid activity (P < 0.001); CB-181963 = quinupristin-dalfopristin = vancomycin > linezolid (P < 0.05); CB-181963 > linezolid (P = 0.003); and CB-181963 = quinupristin-dalfopristin = vancomycin . CB-181963 may provide an alternative treatment for multidrug-resistant staphylococci .

Biotransformation of Explosives by the Old Yellow Enzyme Family of Flavoproteins.
Richard E. Williams, 2004.Several independent studies of bacterial degradation of nitrate ester explosives have demonstrated the involvement of flavin-dependent oxidoreductases related to the old yellow enzyme (OYE) of yeast . Some of these enzymes also transform the nitroaromatic explosive 2,4,6-trinitrotoluene (TNT) . In this work, catalytic capabilities of five members of the OYE family were compared, with a view to correlating structure and function . The activity profiles of the five enzymes differed substantially; no one compound proved to be a good substrate for all five enzymes . TNT is reduced, albeit slowly, by all five enzymes . The nature of the transformation products differed, with three of the five enzymes yielding products indicative of reduction of the aromatic ring . Our findings suggest two distinct pathways of TNT transformation, with the initial reduction of TNT being the key point of difference between the enzymes . Characterization of an active site mutant of one of the enzymes suggests a structural basis for this difference .

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Last modified: May 25, 2005