Shioda M, Kano K, Kobayashi M, Kitagawa I, Shoji M, Yoshida S, Ikegami S
Department of Physiological Chemistry and Nutrition, Faculty of Medicine, University of Tokyo, Japan.
FEBS Lett. 1994 Aug 22;350(2-3):249-52. doi: 10.1016/0014-5793(94)00777-2.
Halenaquinol sulfate, a p-hydroquinone sulfate obtained from a marine sponge, inhibited the activity of eukaryotic DNA polymerases in varying degrees; the Ki values for DNA polymerases, alpha, beta, delta and epsilon were 1.3, 80, 17.5 and 2.0 microM, respectively, whereas it was less effective against E. coli DNA polymerase I. The inhibition occurred competitively with each of dATP and dTTP, but non-competitively with dCTP, dGTP and the template DNA. Thus, halenaquinol sulfate is demonstrated to be a potential inhibitor of DNA polymerases alpha and epsilon, and be a useful tool for analyzing the dNTP binding sites of DNA polymerases.
硫酸卤萘醌是一种从海洋海绵中提取的对苯二酚硫酸盐，它能不同程度地抑制真核生物DNA聚合酶的活性；DNA聚合酶α、β、δ和ε的Ki值分别为1.3、80、17.5和2.0微摩尔，而它对大肠杆菌DNA聚合酶I的抑制作用较弱。这种抑制作用与dATP和dTTP均呈竞争性，但与dCTP、dGTP和模板DNA呈非竞争性。因此，硫酸卤萘醌被证明是DNA聚合酶α和ε的潜在抑制剂，也是分析DNA聚合酶dNTP结合位点的有用工具。
