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Purification and biochemical characterization of IMP-13 metallo-beta-lactamase.

ABSTRACT: The IMP-13 metallo-?-lactamase was overproduced in Escherichia coli BL21(DE3) and purified by chromatography. Analysis of kinetic parameters revealed some notable differences with other IMP-type enzymes, noteworthily a higher catalytic efficiency toward ticarcillin and piperacillin and a marked preference for imipenem over meropenem.

SUBMITTER: Santella G 

PROVIDER: S-EPMC3019620 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Purification and biochemical characterization of IMP-13 metallo-beta-lactamase.

Santella Gisela G   Docquier Jean-Denis JD   Gutkind Gabriel G   Rossolini Gian Maria GM   Radice Marcela M  

Antimicrobial agents and chemotherapy 20101025 1

The IMP-13 metallo-β-lactamase was overproduced in Escherichia coli BL21(DE3) and purified by chromatography. Analysis of kinetic parameters revealed some notable differences with other IMP-type enzymes, noteworthily a higher catalytic efficiency toward ticarcillin and piperacillin and a marked preference for imipenem over meropenem. ...[more]

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