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Updated: Feb 6, 2026

The Use of a β-lactamase-based Conductimetric Biosensor Assay to Detect Biomolecular Interactions
Published on: February 1, 2018
Genetic and Biochemical Characterization of OXA-535, a Distantly Related OXA-48-Like β-Lactamase
L Dabos1,2, A B Jousset1,2,3,4, R A Bonnin1,2,4
1EA7361 "Structure, Dynamic, Function and Expression of Broad Spectrum β-Lactamases," Paris-Sud University, Faculty of Medicine, Le Kremlin-Bicêtre, France.
Abstract:
OXA-535 is a chromosome-encoded carbapenemase of Shewanella bicestrii JAB-1 that shares only 91.3% amino acid sequence identity with OXA-48. Catalytic efficiencies are similar to those of OXA-48 for most β-lactams, except for ertapenem, where a 2,000-fold-higher efficiency was observed with OXA-535. OXA-535 and OXA-436, a plasmid-encoded variant of OXA-535 differing by three amino acids, form a novel cluster of distantly related OXA-48-like carbapenemases. Comparison of blaOXA-535 and blaOXA-436 genetic environments suggests that an ISCR1 may be responsible for blaOXA-436 gene mobilization from the chromosome of Shewanella spp. to plasmids.
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