编码质粒介导的A类头孢噻肟水解β-内酰胺酶（CTX-M-4）的基因序列：丝氨酸237在头孢菌素水解中的作用
Sequence of the gene encoding a plasmid-mediated cefotaxime-hydrolyzing class A beta-lactamase (CTX-M-4): involvement of serine 237 in cephalosporin hydrolysis.
作者信息
Gazouli M, Tzelepi E, Sidorenko S V, Tzouvelekis L S
机构信息
Department of Bacteriology, Hellenic Pasteur Institute, Athens, Greece.
出版信息
Antimicrob Agents Chemother. 1998 May;42(5):1259-62. doi: 10.1128/AAC.42.5.1259.
Abstract
The sequence of the gene encoding a novel cefotaxime-hydrolyzing beta-lactamase (CTX-M-4) was determined. It was located in a plasmid harbored by a Salmonella typhimurium strain. CTX-M-4 was similar to the plasmidic cefotaxime-hydrolyzing beta-lactamases CTX-M-2 and Toho-1 and related to the chromosomal beta-lactamase of Klebsiella oxytoca. A Ser-237-->Ala substitution, introduced by site-directed mutagenesis, caused minor alterations in the interaction of CTX-M-4 with beta-lactams, reducing slightly the relative hydrolytic activity against cefotaxime and the susceptibility to inhibition by clavulanate.
摘要
测定了编码一种新型头孢噻肟水解β-内酰胺酶（CTX-M-4）的基因序列。它位于鼠伤寒沙门氏菌菌株携带的质粒中。CTX-M-4与质粒型头孢噻肟水解β-内酰胺酶CTX-M-2和Toho-1相似，并与产酸克雷伯菌的染色体β-内酰胺酶相关。通过定点诱变引入的Ser-237→Ala取代，导致CTX-M-4与β-内酰胺相互作用的微小变化，略微降低了对头孢噻肟的相对水解活性以及对克拉维酸抑制的敏感性。
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