Abstract
Two new natural CphA metallo-β-lactamases, the CphA4 and CphA5 enzymes, were identified in water samples from municipal sewage in central Italy. Compared to CphA, the CphA4 and CphA5 enzymes showed numerous point mutations. These enzymes have a narrow spectrum of substrates focused on carbapenems only. CphA5 showed kcat values about 40-, 12-, and 97-fold higher than those observed for CphA4 versus imipenem, ertapenem, and biapenem, respectively.
Copyright © 2015, American Society for Microbiology. All Rights Reserved.
MeSH terms
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Aeromonas hydrophila / drug effects
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Aeromonas hydrophila / enzymology*
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Aeromonas hydrophila / genetics
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Amino Acid Sequence
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Anti-Bacterial Agents / pharmacology
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Bacterial Proteins / genetics*
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Carbapenems / pharmacology
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Ertapenem
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Imipenem / pharmacology
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Italy
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Molecular Sequence Data
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Point Mutation / genetics
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Sewage / microbiology*
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Thienamycins / pharmacology
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beta-Lactamases / genetics*
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beta-Lactams / pharmacology
Substances
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Anti-Bacterial Agents
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Bacterial Proteins
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Carbapenems
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Sewage
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Thienamycins
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beta-Lactams
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Imipenem
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beta-Lactamases
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cphA protein, Aeromonas hydrophila
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Ertapenem
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biapenem
Associated data
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GENBANK/KM609958
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GENBANK/KP771880
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PDB/1X8G