ArticleAngewandte Chemie (International ed. in English)2018
A New Mechanism for β-Lactamases: Class D Enzymes Degrade 1β-Methyl Carbapenems through Lactone Formation.
Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 35 citations in OpenAlex.
- SAND: a comprehensive annotation of class D β-lactamases using structural alignment-based numbering.Antimicrobial agents and chemotherapy · 2025Article
- Drug Discovery in the Field of β-Lactams: An Academic Perspective.Antibiotics (Basel, Switzerland) · 2024Review
- β-Lactams from the Ocean.Marine drugs · 2023Review
- Preferred β-lactone synthesis can explain high rate of false-negative results in the detection of OXA-48-like carbapenemases.Scientific reports · 2022Article
- Article
- Multiscale Simulations Identify Origins of Differential Carbapenem Hydrolysis by the OXA-48 β-Lactamase.ACS catalysis · 2022Article
- Studies on the Reactions of Biapenem with VIM Metallo β-Lactamases and the Serine β-Lactamase KPC-2.Antibiotics (Basel, Switzerland) · 2022Article
- Structural and Functional Characterization of OXA-48: Insight into Mechanism and Structural Basis of Substrate Recognition and Specificity.International journal of molecular sciences · 2021Article
- β-Lactam antibiotic targets and resistance mechanisms: from covalent inhibitors to substrates.RSC medicinal chemistry · 2021Review
- Arginine Modulates Carbapenem Deactivation by OXA-24/40 in Acinetobacter baumannii.Journal of molecular biology · 2021Article
- Competing off-loading mechanisms of meropenem from an l,d-transpeptidase reduce antibiotic effectiveness.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Antimicrobial Resistance Conferred by OXA-48 β-Lactamases: Towards a Detailed Mechanistic Understanding.Antimicrobial agents and chemotherapy · 2021Review
- Faropenem reacts with serine and metallo-β-lactamases to give multiple products.European journal of medicinal chemistry · 2021Article
- Analysis of β-lactone formation by clinically observed carbapenemases informs on a novel antibiotic resistance mechanism.The Journal of biological chemistry · 2020Article
- Both the mono- and di-anions of ellagic acid are effective inhibitors of the serine β-lactamase CTX-M-15.RSC advances · 2019Article
- Mechanistic Insights into β-Lactamase-Catalysed Carbapenem Degradation Through Product Characterisation.Scientific reports · 2019Article
- Article
- β-Lactamases and β-Lactamase Inhibitors in the 21st Century.Journal of molecular biology · 2019Review
- Non-Hydrolytic β-Lactam Antibiotic Fragmentation by l,d-Transpeptidases and Serine β-Lactamase Cysteine Variants.Angewandte Chemie (International ed. in English) · 2019Article
- A New Mechanism for β-Lactamases: Class D Enzymes Degrade 1β-Methyl Carbapenems through Lactone Formation.Angewandte Chemie (International ed. in English) · 2018Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
β-Lactamases threaten the clinical use of carbapenems, which are considered antibiotics of last resort. The classical mechanism of serine carbapenemase catalysis proceeds through hydrolysis of an acyl-enzyme intermediate. We show that class D β-lactamases also degrade clinically used 1β-methyl-substituted carbapenems through the unprecedented formation of a carbapenem-derived β-lactone. β-Lactone formation results from nucleophilic attack of the carbapenem hydroxyethyl side chain on the ester carbonyl of the acyl-enzyme intermediate. The carbapenem-derived lactone products inhibit both serine β-lactamases (particularly class D) and metallo-β-lactamases. These results define a new mechanism for the class D carbapenemases, in which a hydrolytic water molecule is not required.
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Registered trials
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.