A new SHV-derived extended-spectrum beta-lactamase (SHV-24) that hydrolyzes ceftazidime through a single-amino-acid substitution (D179G) in the Omega-loop

Authors
Kurokawa, H Yagi, T Shibata, N Shibayama, K Kamachi, K Arakawa, Y
Citation
H. Kurokawa et al., A new SHV-derived extended-spectrum beta-lactamase (SHV-24) that hydrolyzes ceftazidime through a single-amino-acid substitution (D179G) in the Omega-loop, ANTIM AG CH, 44(6), 2000, pp. 1725-1727
Citations number
16
Categorie Soggetti
Microbiology
Journal title
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
ISSN journal
00664804 → ACNP
Volume
44
Issue
6
Year of publication
2000
Pages
1725 - 1727
Database
ISI
SICI code
0066-4804(200006)44:6<1725:ANSEB(>2.0.ZU;2-Y
Abstract
A new SHV-derived extended-spectrum p-lactamase (SHV-24) conferring high-le vel resistance to ceftazidime but not cefotaxime and cefazolin was identifi ed 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 mu M, respectively. SHV-24 was found to have a D179G subst itution in the Omega-loop of the enzyme.