ArticleAntimicrobial agents and chemotherapy2011
Biochemical and structural characterization of the subclass B1 metallo-β-lactamase VIM-4.
Article in Antimicrobial agents and chemotherapy, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.
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Who cites it
29 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance.International journal of molecular sciences · 2015Pooled it
- Mutation of an active site-adjacent residue in VIM indirectly dictates interactions with and blunts inhibition by D-captopril.Journal of inorganic biochemistry · 2025Article
- Genetic diversity, biochemical properties, epidemiology, and detection methods of IMP- and VIM-type carbapenemases.Clinical microbiology reviews · 2025Review
- Article
- Detection and Characterization of VIM-52, a New Variant of VIM-1 from a Klebsiella pneumoniae Clinical Isolate.Antimicrobial agents and chemotherapy · 2021Article
- A Novel Cooperative Metallo-β-Lactamase Fold Metallohydrolase from Pathogen Vibrio vulnificus Exhibits β-Lactam Antibiotic-Degrading Activities.Antimicrobial agents and chemotherapy · 2021Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- 4-(Biomolecules · 2020Article
- Crystal structures of VIM-1 complexes explain active site heterogeneity in VIM-class metallo-β-lactamases.The FEBS journal · 2019Article
- Article
- Interaction of Avibactam with Class B Metallo-β-Lactamases.Antimicrobial agents and chemotherapy · 2016Article
- The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-Lactamase.The Journal of biological chemistry · 2016Article
- B1-Metallo-β-Lactamases: Where Do We Stand?Current drug targets · 2016Review
- Structural Basis of Metallo-β-Lactamase Inhibition by Captopril Stereoisomers.Antimicrobial agents and chemotherapy · 2016Article
- Comparison of Verona Integron-Borne Metallo-β-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition Profiles.Antimicrobial agents and chemotherapy · 2015Article
- Exploring the Role of Residue 228 in Substrate and Inhibitor Recognition by VIM Metallo-β-lactamases.Biochemistry · 2015Article
- His224 alters the R2 drug binding site and Phe218 influences the catalytic efficiency of the metallo-β-lactamase VIM-7.Antimicrobial agents and chemotherapy · 2014Article
- Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution.Antibiotics (Basel, Switzerland) · 2014Article
- A case study comparing quantitative stability-flexibility relationships across five metallo-β-lactamases highlighting differences within NDM-1.Methods in molecular biology (Clifton, N.J.) · 2014Article
- A convenient method to screen for carbapenemase-producing Pseudomonas aeruginosa.Journal of clinical microbiology · 2013Article
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11 authors.
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Abstract
The metallo-β-lactamase VIM-4, mainly found in Pseudomonas aeruginosa or Acinetobacter baumannii, was produced in Escherichia coli and characterized by biochemical and X-ray techniques. A detailed kinetic study performed in the presence of Zn²+ at concentrations ranging from 0.4 to 100 μM showed that VIM-4 exhibits a kinetic profile similar to the profiles of VIM-2 and VIM-1. However, VIM-4 is more active than VIM-1 against benzylpenicillin, cephalothin, nitrocefin, and imipenem and is less active than VIM-2 against ampicillin and meropenem. The crystal structure of the dizinc form of VIM-4 was solved at 1.9 Å. The sole difference between VIM-4 and VIM-1 is found at residue 228, which is Ser in VIM-1 and Arg in VIM-4. This substitution has a major impact on the VIM-4 catalytic efficiency compared to that of VIM-1. In contrast, the differences between VIM-2 and VIM-4 seem to be due to a different position of the flapping loop and two substitutions in loop 2. Study of the thermal stability and the activity of the holo- and apo-VIM-4 enzymes revealed that Zn²+ ions have a pronounced stabilizing effect on the enzyme and are necessary for preserving the structure.
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