Transposition of a Gene Encoding OXA-2 -Lactamase

First report of OXA-143-lactamase producing Acinetobacter baumannii inQom

Objective(s):Antibiotic resistance in Acinetobacter baumannii and outbreaks caused by this organism have been reported from several areas of the world. The present study aimed at determining the antibiotic susceptibility profiles and the distribution of OXA-type beta-lactamases among Iranian Acinetobacter baumannii isolates from Qom of Iran. Materials and Methods: For this study, 108 non-duplic...

Molecular Characterization of a -Lactamase Gene, blaGIM-1, Encoding a New Subclass of Metallo- -Lactamase

OXA-17, a further extended-spectrum variant of OXA-10 beta-lactamase, isolated from Pseudomonas aeruginosa.

Pseudomonas aeruginosa isolates 871 and 873 were isolated at Hacettepe University Hospital in Ankara and were highly resistant to ceftazidime (MIC, 128 microg/ml). Each produced three beta-lactamases, with pIs of 5.3, 6.1, and 7.9. The beta-lactamase with a pI of 5.3 was previously shown to be PER-1 enzyme. The antibiograms of the isolates were not entirely explained by production of PER-1 enzy...

Lysine Carboxylation in Proteins: OXA-10 -Lactamase

An increasing number of proteins are being shown to have an N -carboxylated lysine in their structures, a posttranslational modification of proteins that proceeds without the intervention of a specific enzyme. The role of the carboxylated lysine in theseproteins is typically structural (hydrogen bonding or metal coordination). However, carboxylated lysines in the active sites of OXA-10 and OXA-...

Crystal structure of the class D beta-lactamase OXA-10.

We report the crystal structure of a class D beta-lactamase, the broad spectrum enzyme OXA-10 from Pseudomonas aeruginosa at 2.0 A resolution. There are significant differences between the overall fold observed in this structure and those of the evolutionarily related class A and class C beta-lactamases. Furthermore, the structure suggests the unique, cation mediated formation of a homodimer. K...