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一种新的源自透射电子显微镜(TEM)的超广谱β-内酰胺酶(TEM-91),其ω-环处发生R164C取代,赋予了对头孢他啶的耐药性。

A new TEM-derived extended-spectrum beta-lactamase (TEM-91) with an R164C substitution at the omega-loop confers ceftazidime resistance.

作者信息

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

机构信息

Department of Bacterial Pathogenesis and Infection Control, National Institute of Infectious Diseases, Tokyo, Japan.

出版信息

Antimicrob Agents Chemother. 2003 Sep;47(9):2981-3. doi: 10.1128/AAC.47.9.2981-2983.2003.

Abstract

A new plasmid-mediated TEM-derived extended-spectrum beta-lactamase, TEM-91, was identified in a ceftazidime-resistant (MIC, >128 microg per ml) Escherichia coli strain isolated in 1996 in Japan. TEM-91 has three amino acid substitutions, R164C, M184T, and E240K, compared with TEM-1 penicillinase. The isoelectric point (pI), K(m), and k(cat) of TEM-91 for ceftazidime were 5.7, 179 microM, and 29.0 s(-1), respectively. The K(i) of clavulanic acid for ceftazidime hydrolysis was 30.3 nM.

摘要

1996年在日本分离出的一株对头孢他啶耐药(最低抑菌浓度,>128μg/ml)的大肠杆菌中,鉴定出一种新的质粒介导的源自TEM型的超广谱β-内酰胺酶TEM-91。与TEM-1青霉素酶相比,TEM-91有三个氨基酸取代,即R164C、M184T和E240K。TEM-91对头孢他啶的等电点(pI)、米氏常数(K(m))和催化常数(k(cat))分别为5.7、179μM和29.0 s(-1)。棒酸对头孢他啶水解的抑制常数(K(i))为30.3 nM。

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