Abstract
The non-naturally occurring TEM-1 beta-lactamase mutant R164S:G238S, as well as the R164S (TEM-12) and G238S (TEM-19) beta-lactamases, were constructed and expressed in Escherichia coli under isogenic conditions. Comparison of susceptibilities to beta-lactam antibiotics and substrate profiles showed that the combination of R164S with G238S drastically reduced the extended-spectrum activity of the respective single mutants.
MeSH terms
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Amino Acid Substitution
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Anti-Bacterial Agents / pharmacology*
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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 / metabolism
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Microbial Sensitivity Tests
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Mutagenesis, Site-Directed
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beta-Lactam Resistance / genetics*
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beta-Lactamases / genetics
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beta-Lactamases / metabolism*
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beta-Lactams
Substances
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Anti-Bacterial Agents
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beta-Lactams
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beta-Lactamases
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beta-lactamase TEM-1