Cargando…
Structural and biochemical analysis of the metallo‐β‐lactamase L1 from emerging pathogen Stenotrophomonas maltophilia revealed the subtle but distinct di‐metal scaffold for catalytic activity
Emergence of Enterobacteriaceae harboring metallo‐β‐lactamases (MBL) has raised global threats due to their broad antibiotic resistance profiles and the lack of effective inhibitors against them. We have been studied one of the emerging environmental MBL, the L1 from Stenotrophomonas maltophilia K27...
Autores principales: | Kim, Youngchang, Maltseva, Natalia, Wilamowski, Mateusz, Tesar, Christine, Endres, Michael, Joachimiak, Andrzej |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley & Sons, Inc.
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7020990/ https://www.ncbi.nlm.nih.gov/pubmed/31846104 http://dx.doi.org/10.1002/pro.3804 |
Ejemplares similares
-
Crystal structure of Nsp15 endoribonuclease NendoU from SARS‐CoV‐2
por: Kim, Youngchang, et al.
Publicado: (2020) -
Time-resolved β-lactam cleavage by L1 metallo-β-lactamase
por: Wilamowski, M., et al.
Publicado: (2022) -
Prevalence and detection of Stenotrophomonas maltophilia carrying metallo-β-lactamase blaL1 in Beijing, China
por: Yang, Zhan, et al.
Publicado: (2014) -
Structure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-Lactamase
por: Kim, Youngchang, et al.
Publicado: (2011) -
Probing substrate binding to Metallo-β-Lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis
por: Carenbauer, Anne L, et al.
Publicado: (2002)