Abstract
Penicillin-binding proteins (PBPs) are involved in the regulation of beta-lactamase expression by determining the level of anhydromuramylpeptides in the periplasmatic space. It was hypothesized that one or more PBPs act as a sensor in the beta-lactamase induction pathway. We have performed induction studies with Escherichia coli mutants lacking one to four PBPs with DD-carboxypeptidase activity. Therefore, we conclude that a strong beta-lactamase inducer must inhibit all DD-carboxypeptidases as well as the essential PBPs 1a, 1b, and/or 2.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins*
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Carboxypeptidases / antagonists & inhibitors
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Carboxypeptidases / physiology
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Carrier Proteins / physiology*
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Enterobacter cloacae / drug effects
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Enterobacter cloacae / enzymology*
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Enzyme Induction
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Hexosyltransferases*
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Microbial Sensitivity Tests
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Muramoylpentapeptide Carboxypeptidase / physiology*
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Penicillin-Binding Proteins
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Peptidyl Transferases*
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beta-Lactamases / biosynthesis*
Substances
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Bacterial Proteins
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Carrier Proteins
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Penicillin-Binding Proteins
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Peptidyl Transferases
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Hexosyltransferases
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Carboxypeptidases
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Muramoylpentapeptide Carboxypeptidase
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AmpC beta-lactamases
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beta-Lactamases