| Literature DB >> 26666948 |
Dereje Dadi Gudeta1, Simona Pollini2, Jean-Denis Docquier2, Valeria Bortolaia1, Gian Maria Rossolini3, Luca Guardabassi4.
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.Entities:
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Year: 2015 PMID: 26666948 PMCID: PMC4775976 DOI: 10.1128/AAC.01924-15
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191