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

Hiroshi Kurokawa; Tetsuya Yagi; Naohiro Shibata; Keigo Shibayama; Kazunari Kamachi; Yoshichika Arakawa

doi:10.1128/AAC.44.6.1725-1727.2000

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

Hiroshi Kurokawa, Tetsuya Yagi, Naohiro Shibata, Keigo Shibayama, Kazunari Kamachi, Yoshichika Arakawa

Research output: Contribution to journal › Article › peer-review

27 Citations (Scopus)

Abstract

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 an Escherichia coli clinical isolate. The pI and K(m) 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.

Original language	English
Pages (from-to)	1725-1727
Number of pages	3
Journal	Antimicrobial agents and chemotherapy
Volume	44
Issue number	6
DOIs	https://doi.org/10.1128/AAC.44.6.1725-1727.2000
Publication status	Published - 2000
Externally published	Yes

All Science Journal Classification (ASJC) codes

Pharmacology
Pharmacology (medical)
Infectious Diseases

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1128/AAC.44.6.1725-1727.2000

Cite this

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abstract = "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 an Escherichia coli clinical isolate. The pI and K(m) 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.",

author = "Hiroshi Kurokawa and Tetsuya Yagi and Naohiro Shibata and Keigo Shibayama and Kazunari Kamachi and Yoshichika Arakawa",

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T1 - A New SHV-derived extended-spectrum β-lactamase (SHV-24) that hydrolyzes ceftazidime through a single-amino-acid substitution (D179G) in the Ω-loop

AU - Kurokawa, Hiroshi

AU - Yagi, Tetsuya

AU - Shibata, Naohiro

AU - Shibayama, Keigo

AU - Kamachi, Kazunari

AU - Arakawa, Yoshichika

PY - 2000

Y1 - 2000

N2 - 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 an Escherichia coli clinical isolate. The pI and K(m) 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.

AB - 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 an Escherichia coli clinical isolate. The pI and K(m) 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.

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

Abstract

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