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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) |
Appears in Collections: | Artículos |
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