A New Mechanism for β-Lactamases: Class D Enzymes Degrade 1β-Methyl Carbapenems through Lactone Formation
Author:
Affiliation:
1. Department of Chemistry; University of Oxford; Oxford OX1 3TA UK
2. School of Cellular and Molecular Medicine; University of Bristol; Bristol BS8 1TD UK
Funder
Medical Research Council
Wellcome Trust
Publisher
Wiley
Subject
General Medicine
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/ange.201711308/fullpdf
Reference23 articles.
1. Carbapenemases: the Versatile β-Lactamases
2. “Stormy waters ahead”: global emergence of carbapenemases
3. Structural Basis for Carbapenem-Hydrolyzing Mechanisms of Carbapenemases Conferring Antibiotic Resistance
4. Structural Basis for Clinical Longevity of Carbapenem Antibiotics in the Face of Challenge by the Common Class A β-Lactamases from the Antibiotic-Resistant Bacteria
5. Structural Basis for Carbapenemase Activity of the OXA-23 β-Lactamase from Acinetobacter baumannii
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1. Studies on the Reactions of Biapenem with VIM Metallo β-Lactamases and the Serine β-Lactamase KPC-2;Antibiotics;2022-03-16
2. 19 F NMR Monitoring of Reversible Protein Post‐Translational Modifications: Class D β‐Lactamase Carbamylation and Inhibition;Chemistry – A European Journal;2019-08-20
3. Non-Hydrolytic β-Lactam Antibiotic Fragmentation by l,d -Transpeptidases and Serine β-Lactamase Cysteine Variants;Angewandte Chemie International Edition;2019-01-21
4. Non-Hydrolytic β-Lactam Antibiotic Fragmentation by l,d -Transpeptidases and Serine β-Lactamase Cysteine Variants;Angewandte Chemie;2019-01-21
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