Cargando…
Boronic Acids as Prospective Inhibitors of Metallo-β-Lactamases: Efficient Chemical Reaction in the Enzymatic Active Site Revealed by Molecular Modeling
Boronic acids are prospective compounds in inhibition of metallo-β-lactamases as they form covalent adducts with the catalytic hydroxide anion in the enzymatic active site upon binding. We compare this chemical reaction in the active site of the New Delhi metallo-β-lactamase (NDM-1) with the hydroly...
Autores principales: | Krivitskaya, Alexandra V., Khrenova, Maria G. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8038151/ https://www.ncbi.nlm.nih.gov/pubmed/33918209 http://dx.doi.org/10.3390/molecules26072026 |
Ejemplares similares
-
Influence of the Active Site Flexibility on the Efficiency of Substrate Activation in the Active Sites of Bi-Zinc Metallo-β-Lactamases
por: Krivitskaya, Alexandra V., et al.
Publicado: (2022) -
Revealing electronic features governing hydrolysis of cephalosporins in the active site of the L1 metallo-β-lactamase
por: Levina, Elena O., et al.
Publicado: (2020) -
Bicyclic Boronate VNRX-5133 Inhibits Metallo- and
Serine-β-Lactamases
por: Krajnc, Alen, et al.
Publicado: (2019) -
Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
por: Brem, Jürgen, et al.
Publicado: (2016) -
Metallo-β-Lactamase Inhibitor Phosphonamidate
Monoesters
por: Palica, Katarzyna, et al.
Publicado: (2022)