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.
|Titolo:||Biochemical characterization of laboratory mutants of extended-spectrum β-lactamase TEM-60|
|Data di pubblicazione:||2004|
|Appare nelle tipologie:||1.1 Articolo in rivista|