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

Research output: Contribution to journalArticlepeer-review


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
Issue number12
Publication statusPublished - Dec 2004

ASJC Scopus subject areas

  • Pharmacology (medical)


Dive into the research topics of 'Biochemical characterization of the THIN-B metallo-β-lactamase of Janthinobacterium lividum'. Together they form a unique fingerprint.

Cite this