Boronic acid transition state inhibitors (BATSIs) with R1 side chains of cefotaxime and ceftazidime were assayed against SRV-1, SHV-2, SHV-5, D104K, and D104K G238S beta-lactamases. The D104K variant was the most susceptible to inhibition by the ceftazidime BATSI (K-i, 730 +/- 80 nM), while the D104K G238S variant was the most susceptible to the cefotaxime BATSI (K-i, 1.1 +/- 0.2 mu M).
Use of novel boronic acid transition state inhibitors to probe substrate affinity in SHV-type extended-spectrum β-lactamases / Thomson, Jm; Prati, Fabio; Bethel, Cr; Bonomo, Ra. - In: ANTIMICROBIAL AGENTS AND CHEMOTHERAPY. - ISSN 0066-4804. - STAMPA. - 51:4(2007), pp. 1577-1579. [10.1128/AAC.01293-06]
Use of novel boronic acid transition state inhibitors to probe substrate affinity in SHV-type extended-spectrum β-lactamases
PRATI, Fabio;
2007
Abstract
Boronic acid transition state inhibitors (BATSIs) with R1 side chains of cefotaxime and ceftazidime were assayed against SRV-1, SHV-2, SHV-5, D104K, and D104K G238S beta-lactamases. The D104K variant was the most susceptible to inhibition by the ceftazidime BATSI (K-i, 730 +/- 80 nM), while the D104K G238S variant was the most susceptible to the cefotaxime BATSI (K-i, 1.1 +/- 0.2 mu M).
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