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Antimicrobial Agents and Chemotherapy, September 2004, p. 3579-3582, Vol. 48, No. 9
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.9.3579-3582.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Biochemical Characterization of Laboratory Mutants of Extended-Spectrum ß-Lactamase TEM-60

Bibiana Caporale,1 Nicola Franceschini,1 Mariagrazia Perilli,1 Bernardetta Segatore,1 Gian Maria Rossolini,2 and Gianfranco Amicosante1*

Dipartimento di Scienze e Tecnologie Biomediche, Università di L'Aquila, L'Aquila,1 Dipartimento di Biologia Molecolare, Università di Siena, Siena, Italy2

Received 24 November 2003/ Returned for modification 20 February 2004/ Accepted 3 May 2004

Three mutants of the extended-spectrum ß-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.

* Corresponding author. Mailing address: Dipartimento di Scienze e Tecnologie Biomediche, Università di L'Aquila, Cattedra di Biochimica Clinica, Loc. Coppito, I-67100 L'Aquila, Italy. Phone: 39 0862 433455. Fax: 39 0862 433433. E-mail: amicosante{at}cc.univaq.it.

Antimicrobial Agents and Chemotherapy, September 2004, p. 3579-3582, Vol. 48, No. 9
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.9.3579-3582.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.





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