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• W2128659165 abstract "ABSTRACT The bla IMP gene coding for the IMP-1 metallo-β-lactamase produced by a Pseudomonas aeruginosa clinical isolate (isolate 101/1477) was overexpressed via a T7 expression system in Escherichia coli BL21(DE3), and its product was purified to homogeneity with a final yield of 35 mg/liter of culture. The structural and functional properties of the enzyme purified from E. coli were identical to those of the enzyme produced by P. aeruginosa . The IMP-1 metallo-β-lactamase exhibits a broad-spectrum activity profile that includes activity against penicillins, cephalosporins, cephamycins, oxacephamycins, and carbapenems. Only monobactams escape its action. The enzyme activity was inhibited by metal chelators, of which 1,10- o -phenanthroline and dipicolinic acid were the most efficient. Two zinc-binding sites were found. The zinc content of the P. aeruginosa 101/1477 metallo-β-lactamase was not pH dependent." @default.
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• W2128659165 date "1999-04-01" @default.
• W2128659165 modified "2023-10-16" @default.
• W2128659165 title "Biochemical Characterization of the <i>Pseudomonas aeruginosa</i> 101/1477 Metallo-β-Lactamase IMP-1 Produced by <i>Escherichia coli</i>" @default.
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• W2128659165 doi "https://doi.org/10.1128/aac.43.4.902" @default.
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