An efficient over-expression system was developed for CTX-M-3 extended-spectrum-β-lactamase. The recombinant enzyme was purified from 1 l of culture to yield 22 mg of pure enzyme. The N-terminal amino acid sequence was determined to be NH 2-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. © 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
Overexpression system and biochemical profile of CTX-M-3 extended-spectrum β-lactamase expressed in Escherichia coli
PERILLI, MARIAGRAZIA;ETTORRE, DANIELA;SEGATORE, Bernardetta;MAZZA, Fernando;AMICOSANTE, Gianfranco
2004-01-01
Abstract
An efficient over-expression system was developed for CTX-M-3 extended-spectrum-β-lactamase. The recombinant enzyme was purified from 1 l of culture to yield 22 mg of pure enzyme. The N-terminal amino acid sequence was determined to be NH 2-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. © 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.File in questo prodotto:
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