ArticleAngewandte Chemie (International ed. in English)2019
Non-Hydrolytic β-Lactam Antibiotic Fragmentation by l,d-Transpeptidases and Serine β-Lactamase Cysteine Variants.
Article in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
- Targeting mycobacterial transpeptidases: evaluating the roles of Ldt and PBP inhibition in suppressingAntimicrobial agents and chemotherapy · 2025Article
- Revitalizing cephalosporins: The promise of β-lactamase inhibitor combinations.GMS hygiene and infection control · 2025Article
- Biochemical and crystallographic studies of L,D-transpeptidase 2 from Mycobacterium tuberculosis with its natural monomer substrate.Communications biology · 2024Article
- Article
- High-throughput screen with the l,d-transpeptidase LdtChemical science · 2023Article
- Structure-Activity Relationship of Penem Antibiotic Side Chains Used against Mycobacteria Reveals Highly Active Compounds.ACS infectious diseases · 2022Article
- Article
- The Chemical Relationship Among Beta-Lactam Antibiotics and Potential Impacts on Reactivity and Decomposition.Frontiers in microbiology · 2022Review
- β-Lactam antibiotic targets and resistance mechanisms: from covalent inhibitors to substrates.RSC medicinal chemistry · 2021Review
- Atypically Modified Carbapenem Antibiotics Display Improved Antimycobacterial Activity in the Absence of β-Lactamase Inhibitors.ACS infectious diseases · 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
- Faropenem reacts with serine and metallo-β-lactamases to give multiple products.European journal of medicinal chemistry · 2021Article
- Amoxicillin Haptenation ofFrontiers in pharmacology · 2021Article
- Analysis of β-lactone formation by clinically observed carbapenemases informs on a novel antibiotic resistance mechanism.The Journal of biological chemistry · 2020Article
- Prediction of NHC-catalyzed chemoselective functionalizations of carbonyl compounds: a general mechanistic map.Chemical science · 2020Article
- A Fluorescence-Based Assay for Screening β-Lactams Targeting the Mycobacterium tuberculosis Transpeptidase LdtChembiochem : a European journal of chemical biology · 2020Article
- Phylogenetic and Biochemical Analyses of Mycobacterial l,d-Transpeptidases Reveal a Distinct Enzyme Class That Is Preferentially Acylated by Meropenem.ACS infectious diseases · 2019Article
- Targeting the Mycobacterium tuberculosis transpeptidase LdtChemical communications (Cambridge, England) · 2019Article
- Non-Hydrolytic β-Lactam Antibiotic Fragmentation by l,d-Transpeptidases and Serine β-Lactamase Cysteine Variants.Angewandte Chemie (International ed. in English) · 2019Article
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Authors and funding
13 authors at 2 institutions in 1 country.
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Abstract
Enzymes often use nucleophilic serine, threonine, and cysteine residues to achieve the same type of reaction; the underlying reasons for this are not understood. While bacterial d,d-transpeptidases (penicillin-binding proteins) employ a nucleophilic serine, l,d-transpeptidases use a nucleophilic cysteine. The covalent complexes formed by l,d-transpeptidases with some β-lactam antibiotics undergo non-hydrolytic fragmentation. This is not usually observed for penicillin-binding proteins, or for the related serine β-lactamases. Replacement of the nucleophilic serine of serine β-lactamases with cysteine yields enzymes which fragment β-lactams via a similar mechanism as the l,d-transpeptidases, implying the different reaction outcomes are principally due to the formation of thioester versus ester intermediates. The results highlight fundamental differences in the reactivity of nucleophilic serine and cysteine enzymes, and imply new possibilities for the inhibition of nucleophilic enzymes.
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