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A Two Amino Acid Duplication, L167E168, in the Ω-Loop Drastically Decreases Carbapenemase Activity of KPC-53, a Natural Class A β-Lactamase. | LitMetric

AI Article Synopsis

  • * Cloning into pBC-SK and pET-24a vectors allowed for testing its antimicrobial susceptibility in E. coli, revealing KPC-53 to be less effective against β-lactams, particularly with a significant 2,000-fold decrease in efficacy against imipenem and meropenem.
  • * Molecular modeling suggests that the duplication alters the enzyme’s catalytic pocket interactions, impacting its flexibility and overall catalytic performance compared to KPC-3.

Article Abstract

KPC-53 enzyme is a natural KPC variant which showed a duplication of L167E168 residues in the Ω-loop structure. The gene was cloned both into pBC-SK and pET-24a vectors, and the recombinant plasmids were transferred by transformation in Escherichia coli competent cells to evaluate the antimicrobial susceptibility and to produce the enzyme. Compared to KPC-3, the KPC-53 was less stable and showed a dramatic reduction of and / versus several β-lactams, in particular carbapenems. Indeed, a 2,000-fold reduction was observed in the values of KPC-53 for imipenem and meropenem. Concerning inhibitors, KPC-53 was susceptible to tazobactam and clavulanic acid but maintained resistance to avibactam. The molecular modeling indicates that the L167E168 duplication in KPC-53 modifies the interactions between residues involved in the catalytic pocket, changing the flexibility of the Ω-loop, which is directly coupled with the catalytic properties of the KPC enzymes.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9211410PMC
http://dx.doi.org/10.1128/aac.02402-21DOI Listing

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