A new SHV-derived extended-spectrum beta-lactamase (SHV-24) that hydrolyzes ceftazidime through a single-amino-acid substitution (D179G) in the -loop.
A new SHV-derived extended-spectrum beta-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 an Escherichia coli clinical isolate. The pI and K(m) for CAZ of this enzyme were 7.5 and 30 microM, respectively. SHV-24 was found to have a D179G substitution in the Omega-loop of the enzyme.
Kurokawa
H
H
Department of Bacterial and Blood Products, National Institute of Infectious Diseases, Tokyo, Japan.
Yagi
T
T
Shibata
N
N
Shibayama
K
K
Kamachi
K
K
Arakawa
Y
Y
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D002442:Ceftazidime / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D001618:beta-Lactamases / Q000235:genetics / Q000378:metabolism*
D002442:Ceftazidime; C410347:beta-lactamase SHV-24; D001618:beta-Lactamases