Revisiting the hydrolysis of ampicillin catalyzed by Temoneira‐1 β‐lactamase, and the effect of Ni(II), Cd(II) and Hg(II)

β‐Lactamases grant resistance to bacteria against β‐lactam antibiotics. The active center of TEM‐1 β‐lactamase accommodates a Ser‐Xaa‐Xaa‐Lys motif. TEM‐1 β‐lactamase is not a metalloenzyme but it possesses several putative metal ion binding sites. The sites composed of His residue pairs chelate bor...

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Detalles Bibliográficos
Autores principales: Nafaee, Zeyad H., Egyed, Viktória, Jancsó, Attila, Tóth, Annamária, Gerami, Adeleh Mokhles, Dang, Thanh Thien, Heiniger‐Schell, Juliana, Hemmingsen, Lars, Hunyadi‐Gulyás, Éva, Peintler, Gábor, Gyurcsik, Béla
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Inc. 2023
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10661098/
https://www.ncbi.nlm.nih.gov/pubmed/37853808
http://dx.doi.org/10.1002/pro.4809

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10661098/
https://www.ncbi.nlm.nih.gov/pubmed/37853808
http://dx.doi.org/10.1002/pro.4809

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