Natural Variants of the KPC-2 Carbapenemase have Evolved Increased Catalytic Efficiency for Ceftazidime Hydrolysis at the Cost of Enzyme Stability

por Mehta, Shrenik C., Rice, Kacie, Palzkill, Timothy
Publicado 2015

Deep Sequencing of Random Mutant Libraries Reveals the Active Site of the Narrow Specificity CphA Metallo-β-Lactamase is Fragile to Mutations

por Sun, Zhizeng, Mehta, Shrenik C., Adamski, Carolyn J., Gibbs, Richard A., Palzkill, Timothy
Publicado 2016

KPC-2 β-lactamase enables carbapenem antibiotic resistance through fast deacylation of the covalent intermediate

por Mehta, Shrenik C., Furey, Ian M., Pemberton, Orville A., Boragine, David M., Chen, Yu, Palzkill, Timothy
Publicado 2020

Local interactions with the Glu166 base and the conformation of an active site loop play key roles in carbapenem hydrolysis by the KPC-2 β-lactamase

por Furey, Ian M., Mehta, Shrenik C., Sankaran, Banumathi, Hu, Liya, Prasad, B.V. Venkataram, Palzkill, Timothy
Publicado 2021