Abstract
Extended-spectrum AmpC beta-lactamases of Enterobacteriaceae, which are chromosomally or plasmid-encoded, possess structural modifications in the vicinity of the active site compared with their progenitors. They display an increased catalytic efficiency against extended-spectrum beta-lactams, such as ceftazidime, cefotaxime, cefepime, cefpirome and, in some cases, also against imipenem. An overview of the molecular and biochemical characterization of this recently identified mechanism of resistance to beta-lactams is provided as well as its prevalence and possible clinical significance.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Cephalosporinase / chemistry
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Cephalosporinase / genetics
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Cephalosporinase / metabolism*
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Enterobacteriaceae / drug effects
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Enterobacteriaceae / enzymology
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Enterobacteriaceae / genetics
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Enterobacteriaceae Infections / diagnosis
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Enterobacteriaceae Infections / epidemiology
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Models, Molecular
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Molecular Structure
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Protein Binding
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Protein Structure, Secondary
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beta-Lactam Resistance / genetics
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beta-Lactamases / chemistry
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beta-Lactamases / genetics
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beta-Lactamases / metabolism*
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beta-Lactams / chemistry
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beta-Lactams / metabolism*
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beta-Lactams / pharmacology
Substances
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Bacterial Proteins
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beta-Lactams
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Cephalosporinase
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AmpC beta-lactamases
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beta-Lactamases