CPS-1 is a subclass B3 metallo-β-lactamase from a Chryseobacterium piscium isolate collected from soil, showing 68% amino acid identity to the GOB-1 enzyme. CPS-1 was overproduced in Escherichia coli Rosetta (DE3), purified by chromatography, and biochemically characterized. This enzyme exhibits a broad-spectrum substrate profile, including penicillins, cephalosporins, and carbapenems, which overall resembles those of L1, GOB-1, and acquired subclass B3 enzymes AIM-1 and SMB-1.
Gudeta, D.D., Pollini, S., Docquier, J.D., Bortolaia, V., Rossolini, G.M., Guardabassi, L. (2016). Biochemical characterization of CPS-1, a subclass B3 metallo-β-lactamase from a Chryseobacterium piscium soil isolate. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 60(3), 1869-1873 [10.1128/AAC.01924-15].
Biochemical characterization of CPS-1, a subclass B3 metallo-β-lactamase from a Chryseobacterium piscium soil isolate
POLLINI, SIMONA;DOCQUIER, JEAN DENIS;ROSSOLINI, GIAN MARIA;
2016-01-01
Abstract
CPS-1 is a subclass B3 metallo-β-lactamase from a Chryseobacterium piscium isolate collected from soil, showing 68% amino acid identity to the GOB-1 enzyme. CPS-1 was overproduced in Escherichia coli Rosetta (DE3), purified by chromatography, and biochemically characterized. This enzyme exhibits a broad-spectrum substrate profile, including penicillins, cephalosporins, and carbapenems, which overall resembles those of L1, GOB-1, and acquired subclass B3 enzymes AIM-1 and SMB-1.
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https://hdl.handle.net/11365/1008816
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