Portugal J
Departamento de Biología Molecular y Celular, Consejo Superior de Investigaciones Científicas, Barcelona, Spain.
FEBS Lett. 1994 May 16;344(2-3):136-8. doi: 10.1016/0014-5793(94)00363-7.
The ability of the anti-trypanosomal drug berenil to interfere with the activities of eukaryotic type II topoisomerases is evaluated using two different types of reactions catalyzed by the enzyme: the relaxation of naturally supercoiled DNA and the decatenation of kinetoplast DNA (kDNA). The results indicate that berenil acts as an inhibitor of the catalytic activity, but the inhibiting ability appears to be smaller than for other minor-groove binding ligands.
使用由该酶催化的两种不同类型的反应,评估抗锥虫药物贝尼尔干扰真核II型拓扑异构酶活性的能力:天然超螺旋DNA的松弛和动质体DNA(kDNA)的解连环。结果表明,贝尼尔作为催化活性的抑制剂起作用,但其抑制能力似乎比其他小沟结合配体小。