DNA 回旋酶 A 蛋白中的单个点突变极大地降低了氟喹诺酮类药物与回旋酶-DNA 复合物的结合。
A single point mutation in the DNA gyrase A protein greatly reduces binding of fluoroquinolones to the gyrase-DNA complex.
作者信息
Willmott C J, Maxwell A
机构信息
Department of Biochemistry, University of Leicester, United Kingdom.
出版信息
Antimicrob Agents Chemother. 1993 Jan;37(1):126-7. doi: 10.1128/AAC.37.1.126.
Abstract
Binding of the quinolone drug norfloxacin to gyrase and DNA has been investigated. We have detected binding to gyrase-DNA complex but find no significant binding to either gyrase or DNA alone. Enzyme containing gyrase A protein with the mutation Ser-83 to Trp (conferring quinolone resistance) showed greatly reduced drug binding.
摘要
对喹诺酮类药物诺氟沙星与拓扑异构酶和DNA的结合进行了研究。我们检测到它与拓扑异构酶-DNA复合物结合，但发现它与单独的拓扑异构酶或DNA均无明显结合。含有将Ser-83突变为Trp（赋予喹诺酮耐药性）的拓扑异构酶A蛋白的酶显示药物结合大大减少。
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