|Title:||Ceftibuten stability to active-site serine and metallo-ß-lactamases||Authors:||Perilli, Mariagrazia
Tavio-Perez, Maria Del Mar
|Keywords:||Comparative Invitro Activity
|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|
|Appears in Collections:||Artículos|
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