ArticleACS chemical biology2015
Structural Basis for Enhancement of Carbapenemase Activity in the OXA-51 Family of Class D β-Lactamases.
Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 51 citations in OpenAlex.
- The Novel Carbapenem, JDB/PQ-1-219, Has Potent Broad Spectrum Activity against Multi-Drug ResistantACS infectious diseases · 2026Article
- A conserved hub protein required for peptidoglycan remodeling and cell division inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural insights into the activity of carbapenemases: understanding the mechanism of action of current inhibitors and informing the design of new carbapenem adjuvants.RSC medicinal chemistry · 2025Review
- Structural comparison of substrate-binding pockets of serine β-lactamases in classes A, C, and D.Journal of enzyme inhibition and medicinal chemistry · 2025Review
- Diversity in the Common Fold: Structural Insights into Class D β-Lactamases from Gram-Negative Pathogens.Pathogens (Basel, Switzerland) · 2025Article
- Article
- Standardized Residue Numbering and Secondary Structure Nomenclature in the Class D β-Lactamases.ACS infectious diseases · 2025Article
- A microbiological and structural analysis of the interplay between sulbactam/durlobactam and imipenem against penicillin-binding proteins (PBPs) ofAntimicrobial agents and chemotherapy · 2025Article
- Standardized Residue Numbering and Secondary Structure Nomenclature in the Class D β-Lactamases.bioRxiv : the preprint server for biology · 2025Article
- Molecular genotyping reveals multiple carbapenemase genes and unique blaTropical medicine and health · 2024Article
- Structural and Dynamic Features of Acinetobacter baumannii OXA-66 β-Lactamase Explain Its Stability and Evolution of Novel Variants.Journal of molecular biology · 2024Article
- Article
- Precision drug design againstFrontiers in cellular and infection microbiology · 2023Article
- Specific Amino Acid Substitutions in OXA-51-TypeInternational journal of molecular sciences · 2022Article
- Dynamic Gene Clusters Mediating Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2022Article
- OXA-66 structure and oligomerisation of OXAAccess microbiology · 2022Article
- Colistin and Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2021Article
- A surface loop modulates activity of the Bacillus class D β-lactamases.Journal of structural biology · 2020Article
- Structure-based functional fitness analyses of carbapenemase variants identified among pathogenic carbapenem-resistant Gram-negative bacteria.World journal of microbiology & biotechnology · 2020Article
- Carbapenemases: TransformingBiomolecules · 2020Review
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Class D β-lactamases of Acinetobacter baumannii are enzymes of the utmost clinical importance, producing resistance to last resort carbapenem antibiotics. Although the OXA-51-like enzymes constitute the largest family of class D β-lactamases, they are poorly studied and their importance in conferring carbapenem resistance is controversial. We present the detailed microbiological, kinetic, and structural characterization of the eponymous OXA-51 β-lactamase. Kinetic studies show that OXA-51 has low catalytic efficiency for carbapenems, primarily due to the low affinity of the enzyme for these substrates. Structural studies demonstrate that this low affinity results from the obstruction of the enzyme active site by the side chain of Trp222, which presents a transient steric barrier to an incoming carbapenem substrate. The Trp222Met substitution relieves this steric hindrance and elevates the affinity of the mutant enzyme for carbapenems by 10-fold, significantly increasing the levels of resistance to these antibiotics. The ability of OXA-51 to evolve into a robust carbapenemase as the result of a single amino acid substitution may, in the near future, elevate the ubiquitous enzymes of the OXA-51 family to the status of the most deleterious A. baumannii carbapenemases, with dire clinical consequences.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.