New Conformations of Acylation Adducts of Inhibitors of β-Lactamase from Mycobacterium tuberculosis
Author:
Affiliation:
1. Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, Leiden 2333CC, The Netherlands
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
http://pubs.acs.org/doi/pdf/10.1021/acs.biochem.8b01085
Reference53 articles.
1. Three Decades of β-Lactamase Inhibitors
2. Irreversible Inhibition of the Mycobacterium tuberculosis β-Lactamase by Clavulanate
3. Structure of the Covalent Adduct Formed between Mycobacterium tuberculosis β-Lactamase and Clavulanate
4. Novel fragments of clavulanate observed in the structure of the class A -lactamase from Bacillus licheniformis BS3
5. WHO. (2018) Global Tuberculosis Report 2018, ISBN 9789241565646.
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1. A low-barrier proton shared between two aspartates acts as a conformational switch that changes the substrate specificity of the β-lactamase BlaC;International Journal of Biological Macromolecules;2024-10
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