西班牙分离出的一种新型头孢噻肟水解β-内酰胺酶（CTX-M-10）的核苷酸序列及特性
Nucleotide sequence and characterization of a novel cefotaxime-hydrolyzing beta-lactamase (CTX-M-10) isolated in Spain.
作者信息
Oliver A, Pérez-Díaz J C, Coque T M, Baquero F, Cantón R
机构信息
Servicio de Microbiología, Hospital Ramón y Cajal, Madrid, Spain.
出版信息
Antimicrob Agents Chemother. 2001 Feb;45(2):616-20. doi: 10.1128/AAC.45.2.616-620.2001.
Abstract
A cefotaxime-resistant, ceftazidime-susceptible Escherichia coli isolate was obtained from a patient with sepsis in 1997, from which a beta-lactamase with a pI of 8.1 was cloned. Cephaloridine and cefotaxime relative hydrolysis rates were 167 and 81, respectively (penicillin G rate = 100), whereas ceftazidime hydrolysis was not detected. The nucleotide sequence revealed a bla gene related to that coding for CTX-M-3. Despite 21 nucleotide substitutions, only 2 determined amino acid changes (Ala27Val and Arg38Gln). The amino acid sequence identity between this enzyme, designated CTX-M-10, and the chromosomal beta-lactamase of Kluyvera ascorbata was 81%.
摘要
1997年从一名败血症患者身上分离出一株对头孢噻肟耐药、对头孢他啶敏感的大肠杆菌，从中克隆出一种pI为8.1的β-内酰胺酶。头孢菌素和头孢噻肟的相对水解率分别为167和81（青霉素G的水解率=100），而未检测到头孢他啶的水解。核苷酸序列显示一个与编码CTX-M-3的基因相关的bla基因。尽管有21个核苷酸替换，但仅确定有2个氨基酸变化（Ala27Val和Arg38Gln）。这种命名为CTX-M-10的酶与克吕沃氏菌染色体β-内酰胺酶之间的氨基酸序列同一性为81%。
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