| Literature DB >> 9593168 |
P Giakkoupi1, V Miriagou, M Gazouli, E Tzelepi, N J Legakis, L S Tzouvelekis.
Abstract
The effect of replacement of Met-69 by Ile or Val on the properties of the extended-spectrum beta-lactamase SHV-5 was studied. Mutant enzymes were constructed by site-specific mutagenesis and expressed under isogenic conditions in Escherichia coli DH5alpha cells. Compared with SHV-5, the mutant beta-lactamases conferred lower levels of beta-lactam resistance and were less efficient in hydrolyzing ampicillin, cephalothin, and cefotaxime. The substitutions rendered SHV-5 less susceptible to inhibition by clavulanate, sulbactam, and tazobactam; however, the MICs of penicillin-inhibitor combinations remained similar, suggesting an attenuation of penicillinase activity.Entities:
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Year: 1998 PMID: 9593168 PMCID: PMC105805 DOI: 10.1128/AAC.42.5.1281
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191