期刊
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
卷 48, 期 9, 页码 3579-3582出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.48.9.3579-3582.2004
关键词
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Three mutants of the extended-spectrum beta-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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