Timothy Palzkill Lab

Palzkill Lab: Enzyme Structure and Mechanism

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Brown, C.A., Hu, L., Sun, Z., Patel, M.P., Singh, S., Porter, J.R., Sankaran, B., Prasad, B.V.V., Bowman, G.R., and Palzkill, T. (2020). Antagonism between substitutions in β-lactamase explains a path not taken in the evolution of bacterial drug resistance. J. Biol. Chem. 295:7376-7390.

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Mehta, S.C., Furey, I.M., Pemberton, O.A., Boragine, D.M., Chen, Y., and Palzkill, T. (2021). KPC-2 β-lactamase enables carbapenem antibiotic resistance through fast deacylation of the covalent intermediate. J. Biol. Chem. 296:100155.

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Stojanoski, V., Hu, L., Sankaran, B., Wang, F., Tao, P., Prasad, B.V.V., and Palzkill, T. (2021).  Mechanistic basis of OXA-48 β-lactamases’ hydrolysis of carbapenems. ACS Infect. Dis. 7:445-460.

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Furey, I.M., Mehta, S.C., Sankaran, B., Hu, L., Prasad, B.V.V., and Palzkill, T. (2021). 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. J Biol Chem. 296:100799.

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