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Biochemical Characterization of CPS-1, a Subclass B3 Metallo-?-Lactamase from a Chryseobacterium piscium Soil Isolate.

ABSTRACT: CPS-1 is a subclass B3 metallo-?-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.

SUBMITTER: Gudeta DD

PROVIDER: S-EPMC4775976 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature

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Biochemical Characterization of CPS-1, a Subclass B3 Metallo-β-Lactamase from a Chryseobacterium piscium Soil Isolate.

Gudeta Dereje Dadi DD Pollini Simona S Docquier Jean-Denis JD Bortolaia Valeria V Rossolini Gian Maria GM Guardabassi Luca L

Antimicrobial agents and chemotherapy 20151214 3

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. ...[more]

PMID: 26666948

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