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.
Caporale, B., Franceschini, N., Perilli, M., Segatore, B., Rossolini, G.M., Amicosante, G. (2004). Biochemical characterization of laboratory mutants of the TEM-60 extended-spectrum beta-lactamase. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 48(9), 3579-3582 [10.1128/AAC.48.9.3579-3582.2004].
Biochemical characterization of laboratory mutants of the TEM-60 extended-spectrum beta-lactamase
ROSSOLINI G. M.;
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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https://hdl.handle.net/11365/7922
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