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
Keywords: Comparative Invitro Activity
Klebsiella-Pneumoniae
Citrobacter-Diversus
Serratia-Marcescens
Kinetic-Parameters
Spectrum
Strains
Cephalosporins
Ceftazidime
Sequence
Issue Date: 2001
Publisher: 0924-8579
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. (C) 2001 Published by Elsevier Science B.V. and International Society of Chromotherapy. All rights reserved.
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, p. 45-50
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