The Sequence-Activity Relationship between Metallo-β-Lactamases IMP-1, IMP-6, and IMP-25 Suggests an Evolutionary Adaptation to Meropenem Exposure | Zendy

Eleanor M. Liu | Zendy; Kevin M. Pegg | Zendy; Peter Oelschlaeger | Zendy

Open Access

The Sequence-Activity Relationship between Metallo-β-Lactamases IMP-1, IMP-6, and IMP-25 Suggests an Evolutionary Adaptation to Meropenem Exposure

Author(s) -

Eleanor M. Liu,

Kevin M. Pegg,

Peter Oelschlaeger

Publication year - 2012

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.01440-12

Subject(s) - meropenem , biology , enzyme , sequence (biology) , carbapenem , genetics , mutation , microbiology and biotechnology , antibacterial agent , biochemistry , bacteria , antibiotics , gene , antibiotic resistance

Metallo-β-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 β-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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