ArticleACS catalysis2025
Insights into the Enhanced Ceftazidime Hydrolysis by Ent385 AmpC β‑Lactamase from Multiscale Simulations.
Article in ACS catalysis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed.
- A dual-mode aptasensor based on UiO-66-NH₂@MOF-919 for subtype-specific detection of carbapenem-resistant Klebsiella pneumoniae.Mikrochimica acta · 2026Article
- Functional dynamics of water in New Delhi metallo-β-lactamase catalysis.Protein science : a publication of the Protein Society · 2026Article
- Hydrogen-Bonding Changes Cause Differences in Imipenem Breakdown Activity in OXA-48 Variants.Journal of chemical information and modeling · 2026Article
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2 authors.
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Abstract
The emergence of multidrug-resistant bacteria poses a significant threat to public health. Particularly, they are becoming increasingly resistant to β-lactam antibiotics, which are one of the most important drug classes for the treatment of bacterial infections. Ceftazidime-avibactam has shown promising activity against highly drug-resistant bacteria, including carbapenem-resistant Enterobacterales. However, an Ala294-Pro295 deletion in the Class CAmpC β-lactamase can confer reduced susceptibility to these agents. In this study, we investigated the molecular mechanisms underlying the enhanced hydrolysis of ceftazidime by Ent385 AmpC β-lactamase with the deletion using quantum mechanics/molecular mechanics (QM/MM) simulations. We used constant pH molecular dynamics simulations of the β-lactamase-ceftazidime acyl-enzyme complex to verify the likely protonation states, confirming Tyr150 primarily exists as a tyrosinate. We then used QM/MM (DFTB2/ff14SB) umbrella sampling to calculate the reaction-free energy barriers (Δ
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