[en] The THIN-B metallo-β-lactamase, a subclass B3 enzyme produced by the environmental species Janthinobacterium lividum, was overproduced in Escherichia coli by means of a T7-based expression system. The enzyme was purified (>95%) by two ion-exchange chromatography steps and subjected to biochemical analysis. The native THIN-B enzyme is a monomeric protein of 31 kDa. It exhibits the highest catalytic efficiencies with carbapenem substrates and cephalosporins, except for cephaloridine, which acts as a poor inactivator. Individual rate constants for inactivation by chelators were measured, suggesting that inactivation occurred by a mechanism involving formation of a ternary complex.
Docquier, Jean-Denis ; Université de Liège - ULiège > Département des sciences de la vie > Centre d'ingénierie des protéines
Lopizzo, T.; Dipartimento di Biologia Molecolare, Lab. Fisiol. Biotecnologia M., Università di Siena, Siena, Italy
Liberatori, S.; Laboratorio di Proteomica Funzionale, Università di Siena, Siena, Italy
Prenna, M.; Dipto. Biol. Molec., Cell. e Anim., Università di Camerino, Camerino, Italy
Thaller, M. C.; Dipartimento di Biologia, Univ. di Roma Tor Vergata, Rome, Italy
Frère, Jean-Marie ; Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques
Rossolini, G. M.; Dipartimento di Biologia Molecolare, Lab. Fisiol. Biotecnologia M., Università di Siena, Siena, Italy, Dipartimento di Biologia Molecolare, Università di Siena, Policlinico Le Scotte, 53100 Siena, Italy
Language :
English
Title :
Biochemical characterization of the THIN-B metallo-β-lactamase of Janthinobacterium lividum
Publication date :
2004
Journal title :
Antimicrobial Agents and Chemotherapy
ISSN :
0066-4804
eISSN :
1098-6596
Publisher :
American Society for Microbiology, Washington, United States - District of Columbia
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