ArticleJournal of biochemistry2022
Structural insights into the substrate specificity of IMP-6 and IMP-1 metallo-β-lactamases.
Article in Journal of biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 13 citations in OpenAlex.
- Structural and functional characterization of an active site-influencing variant (IMP-1-F218Y) in IMP-1 metallo-β-lactamase.The FEBS journal · 2026Article
- Phenotypic and Genetic Characteristics ofInternational journal of molecular sciences · 2026Article
- The rise and global spread of IMP carbapenemases (1996-2023): a genomic epidemiology study.Nature communications · 2025Article
- Genetic diversity, biochemical properties, epidemiology, and detection methods of IMP- and VIM-type carbapenemases.Clinical microbiology reviews · 2025Review
- Unique Regulation of Sed-1 β-Lactamase inAntibiotics (Basel, Switzerland) · 2025Article
- Cefiderocol "under siege"? Understanding the rise of NDM-mediated resistance to novel agents.Chemical science · 2025Article
- The emerging concern of IMP variants being resistant to the only IMP-type metallo-β-lactamase inhibitor, xeruborbactam.Antimicrobial agents and chemotherapy · 2025Article
- A Novel Metallo-β-Lactamase AMM-1 From Alteromonas mangrovi Reveals a Cryptic Environmental Reservoir of Carbapenem Resistance.Microbial biotechnology · 2025Article
- The rise and global spread of IMP carbapenemases (1996-2023): a genomic epidemiology study.medRxiv : the preprint server for health sciences · 2025Article
- Current Strategy for Targeting Metallo-β-Lactamase with Metal-Ion-Binding Inhibitors.Molecules (Basel, Switzerland) · 2024Review
- The interaction of the azetidine thiazole side chain with the active site loop (ASL) 3 drives the evolution of IMP metallo-β-lactamase against tebipenem.Antimicrobial agents and chemotherapy · 2024Article
- Prevalence of carbapenem-resistant Enterobacterales withJAC-antimicrobial resistance · 2024Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
IMP-type metallo-β-lactamases confer resistance to carbapenems and a broad spectrum of β-lactam antibiotics. IMP-6 and IMP-1 differ by only a point mutation: Ser262 in IMP-1 and Gly262 in IMP-6. The kcat/Km values of IMP-1 for imipenem and meropenem are nearly identical; however, for IMP-6, the kcat/Km for meropenem is 7-fold that for imipenem. In clinical practice, this may result in an ineffective therapeutic regimen and, consequently, in treatment failure. Here, we report the crystal structures of IMP-6 and IMP-1 with the same space group and similar cell constants at resolutions of 1.70 and 1.94 Å, respectively. The overall structures of IMP-6 and IMP-1 are similar. However, the loop region (residues 60-66), which participates in substrate binding, is more flexible in IMP-6 than in IMP-1. This difference in flexibility determines the substrate specificity of IMP-type metallo-β-lactamases for imipenem and meropenem. The amino acid at position 262 alters the mobility of His263; this affects the flexibility of the loop via a hydrogen bond with Pro68, which plays the role of a hinge in IMP-type metallo-β-lactamases. The substitution of Pro68 with a glycine elicited an increase in the Km of IMP-6 for imipenem, whereas the affinity for meropenem remained unchanged.
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