| Literature DB >> 23836186 |
Kevin M Pegg1, Eleanor M Liu, Alecander E Lacuran, Peter Oelschlaeger.
Abstract
IMP-type enzymes constitute a clinically important family of metallo-β-lactamases that has grown dramatically in the past decade to its current 45 known members. Here, we report the biochemical characterization of IMP-30 in comparison to IMP-1, from which it deviates by a single E59K mutation. Kinetics, MIC assays, docking, and molecular dynamics simulations support a scenario in which Lys59 interacts with the ceftazidime R1 group, resulting in increased water access and enhanced turnover and MIC of ceftazidime.Entities:
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Year: 2013 PMID: 23836186 PMCID: PMC3811441 DOI: 10.1128/AAC.02341-12
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191