Three mutants of the extended-spectrum β-lactamase TEM-60, the P51L, K104E, and S164R mutants, were constructed by site-directed mutagenesis. The kinetic parameters of the mutated enzymes and interactions of inhibitors were significantly different from those of TEM-60, revealing that the L51P mutation plays an important role in enzyme activity and stability in the TEM-60 background.

Biochemical characterization of laboratory mutants of extended-spectrum β-lactamase TEM-60

FRANCESCHINI, Nicola;PERILLI, MARIAGRAZIA;SEGATORE, Bernardetta;AMICOSANTE, Gianfranco
2004-01-01

Abstract

Three mutants of the extended-spectrum β-lactamase TEM-60, the P51L, K104E, and S164R mutants, were constructed by site-directed mutagenesis. The kinetic parameters of the mutated enzymes and interactions of inhibitors were significantly different from those of TEM-60, revealing that the L51P mutation plays an important role in enzyme activity and stability in the TEM-60 background.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11697/103023
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