Behaviour of cefmenoxime towards beta-lactamases.
Using several well-characterized beta-lactamases isolated from Gram-negative bacteria, the interactions of cefmenoxime, a new methoxy-imino-amino-2-thiazol cephalosporin were compared with those of cefotaxime, lamoxactam, cefoperazone and ceftazidime. On-line computerized microacidimetry allowed determination of the affinity of these compounds for the enzymes, which was characterized by Ki values. Microacidimetry showed poor interactions of cefmenoxime with penicillinase TEM-1 (low Vm, poor affinity) whereas it showed a high affinity for the cephalosporinases, as is also the case for cefotaxime or lamoxactam. Both cefmenoxime and cefotaxime showed relative susceptibility in Masuda's double disc technique.
D015281:Cefmenoxime; D002439:Cefotaxime / Q000031:analogs & derivatives* / Q000378:metabolism; D002440:Cefoxitin / Q000378:metabolism; D003201:Computers; D004754:Enterobacter / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology; D007700:Kinetics; D007709:Klebsiella / Q000201:enzymology; D009070:Moxalactam / Q000378:metabolism; D011514:Proteus vulgaris / Q000201:enzymology; D011550:Pseudomonas aeruginosa / Q000201:enzymology; D001618:beta-Lactamases / Q000378:metabolism*
D002440:Cefoxitin; D001618:beta-Lactamases; D015281:Cefmenoxime; D002439:Cefotaxime; D009070:Moxalactam