Abstract
Cloning, sequencing, and biochemical analysis identified a novel AmpC-type beta-lactamase conferring resistance to extended-spectrum cephalosporins in an Escherichia coli clinical isolate. This enzyme, exhibiting 14 amino acid substitutions compared to a reference AmpC cephalosporinase of E. coli, hydrolyzed ceftazidime and cefepime significantly.
Publication types
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Case Reports
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Research Support, Non-U.S. Gov't
MeSH terms
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Aged
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Aged, 80 and over
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Amino Acid Sequence
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Amino Acid Substitution
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Cefepime
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Ceftazidime / pharmacology
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Cephalosporin Resistance / genetics*
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Cephalosporins / pharmacology
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Cloning, Molecular
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DNA, Bacterial / genetics
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Escherichia coli / drug effects
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Escherichia coli Infections / microbiology*
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Female
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Humans
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Kinetics
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Molecular Sequence Data
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beta-Lactamases / genetics
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beta-Lactamases / metabolism*
Substances
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Bacterial Proteins
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Cephalosporins
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DNA, Bacterial
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Cefepime
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Ceftazidime
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AmpC beta-lactamases
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beta-Lactamases
Associated data
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GENBANK/AY533244
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GENBANK/AY533245