Cargando…
Structural insights into the substrate specificity of IMP-6 and IMP-1 metallo-β-lactamases
IMP-type metallo-β-lactamases confer resistance to carbapenems and a broad spectrum of β-lactam antibiotics. IMP-6 and IMP-1 differ by only a point mutation: Ser262 in IMP-1 and Gly262 in IMP-6. The k(cat)/K(m) values of IMP-1 for imipenem and meropenem are nearly identical; however, for IMP-6, the...
Autores principales: | Yamamoto, Keizo, Tanaka, Hideaki, Kurisu, Genji, Nakano, Ryuichi, Yano, Hisakazu, Sakai, Hiromi |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9792659/ https://www.ncbi.nlm.nih.gov/pubmed/36174533 http://dx.doi.org/10.1093/jb/mvac080 |
Ejemplares similares
-
IMP-68, a Novel IMP-Type Metallo-β-Lactamase in Imipenem-Susceptible Klebsiella pneumoniae
por: Kubota, Hiroaki, et al.
Publicado: (2019) -
RNA-hydrolyzing activity of metallo-β-lactamase IMP-1
por: Kato, Yoshiki, et al.
Publicado: (2020) -
Characterization of Three Novel IMP Metallo-β-Lactamases, IMP-89, IMP-91, and IMP-96, and Diverse bla(IMP)-Carrying Accessory Genetic Elements from Chinese Clinical Isolates
por: Li, Xinyue, et al.
Publicado: (2023) -
Structure and Molecular Recognition Mechanism of IMP-13 Metallo-β-Lactamase
por: Softley, Charlotte A., et al.
Publicado: (2020) -
Emergence of Citrobacter freundii carrying IMP-8 metallo-β-lactamase in Germany
por: Peter, S, et al.
Publicado: (2014)