DOCQUIER J-D.

FRERE J-M.

G. ROSSOLINI

LIBERATORI S.

LOPIZZO T.

PRENNA M.

THALLER M.C.

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 J. D.

THALLER M. C.

ROSSOLINI G. M.

Archivio della Ricerca - Università degli Studi di Siena

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

Biochemical characterization of the THIN-B metallo-beta-lactamase of Janthinobacterium lividum.

Biochemical characterization of the THIN-B metallo-beta-lactamase of Janthinobacterium lividum.

Abstract

Similar works

Full text

Available Versions

Archivio della Ricerca - Università degli Studi di Siena