Biochemical characterization of laboratory mutants of extended-spectrum beta-lactamase TEM-60.
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.
Dipartimento di Scienze e Tecnologie Biomediche, Università di L'Aquila, Cattedra di Biochimica Clinica, Loc. Coppito, I-67100 L'Aquila, Italy.
Bibiana
B
Caporale
Nicola
N
Franceschini
Mariagrazia
M
Perilli
Bernardetta
B
Segatore
Gian Maria
GM
Rossolini
Gianfranco
G
Amicosante
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D017931:DNA Primers; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D009154:Mutation / Q000235:genetics*; D020133:Reverse Transcriptase Polymerase Chain Reaction; D018440:beta-Lactam Resistance; D001618:beta-Lactamases / Q000235:genetics*
D017931:DNA Primers; D004791:Enzyme Inhibitors; D001618:beta-Lactamases; C492442:beta-lactamase TEM-60, Providencia stuartii