Abstract
Boronic acid transition state inhibitors (BATSIs) with R1 side chains of cefotaxime and ceftazidime were assayed against SHV-1, SHV-2, SHV-5, D104K, and D104K G238S beta-lactamases. The D104K variant was the most susceptible to inhibition by the ceftazidime BATSI (Ki, 730+/-80 nM), while the D104K G238S variant was the most susceptible to the cefotaxime BATSI (Ki, 1.1+/-0.2 microM).
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Anti-Bacterial Agents / pharmacology*
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Boronic Acids / pharmacology*
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Ceftazidime / pharmacology
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Drug Design
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Enzyme Inhibitors / chemical synthesis
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Enzyme Inhibitors / chemistry*
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Substrate Specificity
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beta-Lactamase Inhibitors*
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beta-Lactamases / drug effects
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beta-Lactamases / metabolism
Substances
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Anti-Bacterial Agents
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Boronic Acids
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Enzyme Inhibitors
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beta-Lactamase Inhibitors
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Ceftazidime
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beta-Lactamases