Purification and biochemical characterization of IMP-13 metallo-beta-lactamase.
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.
Santella
Gisela
G
Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Buenos Aires, Argentina.
Docquier
Jean-Denis
JD
Gutkind
Gabriel
G
Rossolini
Gian Maria
GM
Radice
Marcela
M
D000900:Anti-Bacterial Agents / Q000378:metabolism / Q000494:pharmacology*; D004926:Escherichia coli / Q000187:drug effects* / Q000201:enzymology*; D010878:Piperacillin / Q000378:metabolism / Q000494:pharmacology; D013982:Ticarcillin / Q000378:metabolism / Q000494:pharmacology; D001618:beta-Lactamases / Q000302:isolation & purification* / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D001618:beta-Lactamases; D013982:Ticarcillin; D010878:Piperacillin