Please use this identifier to cite or link to this item: http://hdl.handle.net/10553/49969
Title: Overexpression system and biochemical profile of CTX-M-3 extended-spectrum β-lactamase expressed in Escherichia coli
Authors: Perilli, Mariagrazia
Ettorre, Daniela
Segatore, Bernardetta
Caporale, Bibiana
Santis, Francesca De
Pochetti, Giorgio
Brigante, Gioconda
Mazza, Fernando
Tavìo, Marìa M. 
Amicosante, Gianfranco
Keywords: Klebsiella-Pneumoniae
Enterobacteriaceae
Enzyme
Identification
Proteins, et al
Issue Date: 2004
Publisher: 0378-1097
Journal: FEMS Microbiology Letters 
Abstract: 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. (C) 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
URI: http://hdl.handle.net/10553/49969
ISSN: 0378-1097
DOI: 10.1016/j.femsle.2004.10.031
Source: FEMS Microbiology Letters[ISSN 0378-1097],v. 241, p. 229-232
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