Sensitivity of Aeromonas hydrophila carbapenemase to delta3-cephems: comparative study with other metallo-beta-lactamases.
Ceftriaxone and ceftriaxone S-oxide behaved as inactivators against the metallo-beta-lactamase of Aeromonas hydrophila AE036 and as substrates for the zinc beta-lactamase produced by Bacillus cereus (569/H/9) and Stenotrophomonas maltophilia ULA 511. Moreover, RO 09-1428, a catechol-cephalosporin, was not recognized by the A. hydrophila enzyme. Panipenem, cephalosporin C, cephalosporin C-gamma-lactone, and loracarbef were substrates for the three studied beta-lactamases.
Felici
A
A
Dipartimento di Scienze e Tecnologie Biomediche Cattedra di Chimica Biologica e di Enzimologia, Università degli Studi dell'Aquila, Coppito (L'Aquila), Italy.
Perilli
M
M
Franceschini
N
N
Rossolini
G M
GM
Galleni
M
M
Frere
J M
JM
Oratore
A
A
Amicosante
G
G
D016980:Aeromonas hydrophila / Q000187:drug effects / Q000201:enzymology*; D001426:Bacterial Proteins; D003524:Cyclosporins / Q000494:pharmacology*; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D006868:Hydrolysis; D007700:Kinetics; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases
D001426:Bacterial Proteins; D003524:Cyclosporins; D004791:Enzyme Inhibitors; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases; C063912:carbapenemase