Article (Scientific journals)
Sensitivity of Aeromonas hydrophila carbapenemase to delta3-cephems: comparative study with other metallo-beta-lactamases.
Felici, A.; Perilli, M.; Franceschini, N. et al.
1997In Antimicrobial Agents and Chemotherapy, 41 (4), p. 866-8
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Keywords :
Aeromonas hydrophila/drug effects/enzymology; Bacterial Proteins; Cyclosporins/pharmacology; Enzyme Inhibitors/pharmacology; Hydrolysis; Kinetics; beta-Lactamase Inhibitors
Abstract :
[en] 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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Felici, A.
Perilli, M.
Franceschini, N.
Rossolini, G. M.
Galleni, Moreno ;  Université de Liège - ULiège
Frère, Jean-Marie ;  Université de Liège > Département des sciences de la vie > Centre d'ingénierie des protéines
Oratore, A.
Amicosante, G.
Language :
English
Title :
Sensitivity of Aeromonas hydrophila carbapenemase to delta3-cephems: comparative study with other metallo-beta-lactamases.
Publication date :
1997
Journal title :
Antimicrobial Agents and Chemotherapy
ISSN :
0066-4804
eISSN :
1098-6596
Publisher :
American Society for Microbiology, Washington, United States - District of Columbia
Volume :
41
Issue :
4
Pages :
866-8
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 01 December 2015

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