Structure, activity and thermostability investigations of OXA-163, OXA-181 and OXA-245 using biochemical analysis, crystal structures and differential scanning calorimetry analysis.

ABSTRACT: The first crystal structures of the class D β-lactamases OXA-181 and OXA-245 were determined to 2.05 and 2.20 Å resolution, respectively; in addition, the structure of a new crystal form of OXA-163 was resolved to 2.07 Å resolution. All of these enzymes are OXA-48-like and have been isolated from different clinical Klebsiella pneumoniae strains and also from other human pathogens such as Pseudomonas aeruginosa and Escherichia coli. Here, enzyme kinetics and thermostability studies are presented, and the new crystal structures are used to explain the observed variations. OXA-245 had the highest melting point (T_m = 55.8°C), as determined by differential scanning calorimetry, compared with OXA-163 (T_m = 49.4°C) and OXA-181 (T_m = 52.6°C). The differences could

SUBMITTER: Lund BA 

PROVIDER: S-EPMC5633926 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature