A natural TEM variant β-lactamase was isolated from an epidemic strain of Serratia marcescens. Nucleotide gene sequencing revealed multiple point mutations located in the 42-to-44 tripeptide and positions 145 to 146, 178, and 238. In addition, a glutamic acid 212 deletion was also found. The purified enzyme was studied from a kinetic point of view, revealing the highest catalytic efficiency (k(cat)/K(m)) values for ceftazidime and aztreonam compared with the TEM-1 prototype enzyme. The in vitro resistance correlated with kinetic parameters, and the enzyme also mediated resistance to some penicillins and an ampicillin-clavulanic acid combination. The mutational and kinetic changes are discussed in relation to the three- dimensional crystallographic structure of the wild-type TEM-1 enzyme.

Characterization of a new TEM-derived β-lactamase produced in a Serratia marcescens strain

PERILLI, MARIAGRAZIA;FRANCESCHINI, Nicola;ORATORE, Arduino;AMICOSANTE, Gianfranco
1997-01-01

Abstract

A natural TEM variant β-lactamase was isolated from an epidemic strain of Serratia marcescens. Nucleotide gene sequencing revealed multiple point mutations located in the 42-to-44 tripeptide and positions 145 to 146, 178, and 238. In addition, a glutamic acid 212 deletion was also found. The purified enzyme was studied from a kinetic point of view, revealing the highest catalytic efficiency (k(cat)/K(m)) values for ceftazidime and aztreonam compared with the TEM-1 prototype enzyme. The in vitro resistance correlated with kinetic parameters, and the enzyme also mediated resistance to some penicillins and an ampicillin-clavulanic acid combination. The mutational and kinetic changes are discussed in relation to the three- dimensional crystallographic structure of the wild-type TEM-1 enzyme.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11697/103170
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