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| Título: | Overexpression system and biochemical profile of CTX-M-3 extended-spectrum β-lactamase expressed in Escherichia coli | Autores/as: | Perilli, Mariagrazia Ettorre, Daniela Segatore, Bernardetta Caporale, Bibiana Santis, Francesca De Pochetti, Giorgio Brigante, Gioconda Mazza, Fernando Tavìo, Marìa M. Amicosante, Gianfranco |
Clasificación UNESCO: | 32 Ciencias médicas 320103 Microbiología clínica |
Palabras clave: | Klebsiella-Pneumoniae Enterobacteriaceae Enzyme Identification Proteins, et al. |
Fecha de publicación: | 2004 | Publicación seriada: | FEMS Microbiology Letters | Resumen: | An efficient over-expression system was developed for CTX-M-3 extended-spectrum-beta-lactamase. The recombinant enzyme was purified from 11 of culture to yield 22 mg of pure enzyme. The N-terminal amino acid sequence was determined to be NH2-QTADVQ... Determination of kinetic parameters with the purified CTX-M-3 revealed efficient hydrolysis of penicillins and cephalosporins, while ceftazidime and aztreonam were very poor substrates. Clavulanic acid, sulbactam and especially tazobactam inhibited the CTX-M-3 enzyme. | URI: | http://hdl.handle.net/10553/49969 | ISSN: | 0378-1097 | DOI: | 10.1016/j.femsle.2004.10.031 | Fuente: | FEMS Microbiology Letters[ISSN 0378-1097],v. 241, p. 229-232 |
| Colección: | Artículos |
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