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

H Kurokawa; T Yagi; N Shibata; K Shibayama; K Kamachi; Y Arakawa

doi:10.1128/AAC.44.6.1725-1727.2000

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

Antimicrob Agents Chemother. 2000 Jun;44(6):1725-7. doi: 10.1128/AAC.44.6.1725-1727.2000.

Authors

H Kurokawa¹, T Yagi, N Shibata, K Shibayama, K Kamachi, Y Arakawa

Affiliation

¹ Department of Bacterial and Blood Products, National Institute of Infectious Diseases, Tokyo, Japan.

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Amino Acid Substitution
Ceftazidime / metabolism*
Escherichia coli / enzymology*
Hydrolysis
Molecular Sequence Data
beta-Lactamases / genetics
beta-Lactamases / metabolism*

Substances

Ceftazidime
beta-lactamase SHV-24
beta-Lactamases

Associated data

GENBANK/AB023477