Open AccessA New SHV-Derived Extended-Spectrum β-Lactamase (SHV-24) That Hydrolyzes Ceftazidime through a Single-Amino-Acid Substitution (D179G) in the Ω-Loop
Author(s) -
Hiroshi Kurokawa,
Tetsuya Yagi,
Naohiro Shibata,
Keigo Shibayama,
Kazunari Kamachi,
Yoshichika Arakawa
Publication year - 2000
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.44.6.1725-1727.2000
Subject(s) - ceftazidime , cefotaxime , cefazolin , escherichia coli , plasmid , enzyme , microbiology and biotechnology , biology , enterobacteriaceae , beta lactamase , amino acid substitution , antibiotics , biochemistry , bacteria , genetics , dna , mutation , gene , pseudomonas aeruginosa
A new SHV-derived extended-spectrum β-lactamase (SHV-24) conferring high-level resistance to ceftazidime but not cefotaxime and cefazolin was identified in Japan. This enzyme was encoded by a transferable 150-kb plasmid from anEscherichia coli clinical isolate. The pI andKm for CAZ of this enzyme were 7.5 and 30 μM, respectively. SHV-24 was found to have a D179G substitution in the Ω-loop of the enzyme.