ArticleAntimicrobial agents and chemotherapy2013
Biochemical characterization of IMP-30, a metallo-β-lactamase with enhanced activity toward ceftazidime.
Article in Antimicrobial agents and chemotherapy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Genetic diversity, biochemical properties, epidemiology, and detection methods of IMP- and VIM-type carbapenemases.Clinical microbiology reviews · 2025Review
- Active site loops of membrane-anchored metallo-β-lactamases from environmental bacteria determine cephalosporinase activity.Antimicrobial agents and chemotherapy · 2025Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Carbapenem Use Is Driving the Evolution of Imipenemase 1 Variants.Antimicrobial agents and chemotherapy · 2021Article
- B1-Metallo-β-Lactamases: Where Do We Stand?Current drug targets · 2016Review
- Elucidating the Role of Residue 67 in IMP-Type Metallo-β-Lactamase Evolution.Antimicrobial agents and chemotherapy · 2015Article
- Epidemiology and Characteristics of Metallo-β-Lactamase-Producing Pseudomonas aeruginosa.Infection & chemotherapy · 2015Review
- Understanding the determinants of substrate specificity in IMP family metallo-β-lactamases: the importance of residue 262.Protein science : a publication of the Protein Society · 2014Article
- Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution.Antibiotics (Basel, Switzerland) · 2014Article
- New β-phospholactam as a carbapenem transition state analog: Synthesis of a broad-spectrum inhibitor of metallo-β-lactamases.Bioorganic & medicinal chemistry letters · 2013Article
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Authors and funding
4 authors.
Funding
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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.
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