Open AccessOXA-14, another extended-spectrum variant of OXA-10 (PSE-2) beta-lactamase from Pseudomonas aeruginosa
Author(s) -
Franck Danel,
Lucinda M. C. Hall,
Deniz Gür,
David M. Livermore
Publication year - 1995
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.39.8.1881
Subject(s) - pseudomonas aeruginosa , beta lactamase , glycine , beta (programming language) , beta lactam , microbiology and biotechnology , pseudomonadales , pseudomonadaceae , plasmid , chemistry , biology , antibiotics , bacteria , escherichia coli , biochemistry , amino acid , gene , genetics , computer science , programming language
Pseudomonas aeruginosa 455, isolated in Ankara, Turkey, produced a pI 6.2 beta-lactamase determined by plasmid pMLH53 and resisted all beta-lactams except carbapenems. This beta-lactamase, named OXA-14, corresponded to OXA-10 (PSE-2) except that aspartate replaced glycine at position 157 and thus is intermediate between OXA-10 and OXA-11, which has aspartate at position 157 and a further substitution at position 143.