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Article

A drug-resistant β-lactamase variant changes the conformation of its active-site proton shuttle to alter substrate specificity and inhibitor potency.

The Journal of biological chemistry - 25 Dec 2020

Soeung Victoria, Lu Shuo, Hu Liya, Judge Allison, Sankaran Banumathi, Prasad B V Venkataram, Palzkill Timothy

Abstract excerpt

Lys234 is one of the residues present in class A β-lactamases that is under selective pressure due to antibiotic use. Located adjacent to proton shuttle residue Ser130, it is suggested to play a role in proton transfer during catalysis of the antibiotics. The mechanism underpinning how substitutions in this position modulate inhibitor efficiency and substrate specificity leading to drug resistance is unclear. The...

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PMID: 33109613
DOI: 10.1074/jbc.RA120.016103

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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