Characterization of the 2-[(R)-2-Hydroxypropylthio]ethanesulfonate Dehydrogenase fromXanthobacterStrain Py2:  Product Inhibition, pH Dependence of Kinetic Parameters, Site-Directed Mutagenesis, Rapid Equilibrium Inhibition, and Chemical Modification†

Biochemistry ◽  
2002 ◽  
Vol 41 (8) ◽  
pp. 2727-2740 ◽  
Author(s):  
Daniel D. Clark ◽  
Scott A. Ensign
Keyword(s):  
Chemical Modification ◽  
Kinetic Parameters ◽  
Ph Dependence ◽  
Product Inhibition ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Rapid Equilibrium

scholarly journals Biochemical Characterization of Laboratory Mutants of Extended-Spectrum β-Lactamase TEM-60

2004 ◽  
Vol 48 (9) ◽  
pp. 3579-3582 ◽  
Author(s):  
Bibiana Caporale ◽  
Nicola Franceschini ◽  
Mariagrazia Perilli ◽  
Bernardetta Segatore ◽  
Gian Maria Rossolini ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Kinetic Parameters ◽  
Biochemical Characterization ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Extended Spectrum

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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