Please use this identifier to cite or link to this item: http://hdl.handle.net/10553/49972
Title: Ceftibuten stability to active-site serine and metallo-ß-lactamases
Authors: Perilli, Mariagrazia
Segatore, Bernardetta
Franceschini, Nicola
Gizzi, Giovanni
Mancinelli, Andrea
Caravelli, Berardo
Setacci, Domenico
Tavio-Perez, Maria Del Mar 
Bianchi, Bruno
Amicosante, Gianfranco
UNESCO Clasification: 32 Ciencias médicas
320103 Microbiología clínica
Keywords: Ceftibuten
ß-Lactamases
Affinity
Catalytic efficiency
Issue Date: 2001
Journal: International Journal of Antimicrobial Agents 
Abstract: Ceftibuten is an oral third-generation cephalosporin active against a wide range of bacteria and shows an improved stability to hydrolysis by several beta -lactamases because of the carboxyethilidine moiety at position 7 of the beta -acyl side chain. The kinetic interactions between ceftibuten and active-site serine and metallo-beta -lactamases were investigated. The activity of several TEM-derived extended spectrum beta -lactamases (ES beta Ls) against ceftibuten, cefotaxime and ceftazidime was compared using K-m, K-cat and K-cat/K-m. Ceftibuten behaved as a poor substrate for class A and B beta -lactamases compared with cefotaxime. The chromosomal class C beta -lactamase from Enterobacter cloacae 908R gave a high k(cat) value (21 s(-1)), whereas there was poor activity with enzymes from Acinetobacter baumannii and Morganella morganii and ceftibuten. Ceftibuten resists hydrolysis in the presence of typical respiratory or urogenital-tract pathogens producing beta -lactamases.
URI: http://hdl.handle.net/10553/49972
ISSN: 0924-8579
DOI: 10.1016/S0924-8579(00)00319-8
Source: International Journal of Antimicrobial Agents[ISSN 0924-8579],v. 17(1), p. 45-50 (Enero 2001)
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