Biochemical characterization of the THIN-B metallo-β-lactamase of Janthinobacterium lividum

Jean Denis Docquier, Teresa Lopizzo, Sabrina Liberatori, Manuela Prenna, Maria Cristina Thaller, Jean Marie Frère, Gian Maria Rossolini

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Abstract

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.

Original languageEnglish
Pages (from-to)4778-4783
Number of pages6
JournalAntimicrobial Agents and Chemotherapy
Volume48
Issue number12
DOIs
Publication statusPublished - Dec 2004

ASJC Scopus subject areas

  • Pharmacology (medical)

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    Docquier, J. D., Lopizzo, T., Liberatori, S., Prenna, M., Thaller, M. C., Frère, J. M., & Rossolini, G. M. (2004). Biochemical characterization of the THIN-B metallo-β-lactamase of Janthinobacterium lividum. Antimicrobial Agents and Chemotherapy, 48(12), 4778-4783. https://doi.org/10.1128/AAC.48.12.4778-4783.2004