Journal
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
Volume 56, Issue 12, Pages 6403-6406Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.01440-12
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Funding
- Research Corporation for Science Advancement [10493]
- W. M. Keck Foundation
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Metallo-beta-lactamases are important determinants of antibacterial resistance. In this study, we investigate the sequence-activity relationship between the closely related enzymes IMP-1, IMP-6, and IMP-25. While IMP-1 is the more efficient enzyme across the overall spectrum of tested beta-lactam antibacterial agents, IMP-6 and IMP-25 seem to have evolved to specifically inactivate the newer carbapenem meropenem. Molecular modeling indicates that the G235S mutation distinguishing IMP-25 from IMP-1 and IMP-6 may affect enzyme activity via Asn233.
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