Department of Chemistry and Biochemistry, North Dakota State University, Fargo, ND 58108, USA.
Bioorg Med Chem Lett. 2011 Oct 1;21(19):5920-3. doi: 10.1016/j.bmcl.2011.07.080. Epub 2011 Aug 4.
We report, for the first time, that certain N-acetylthiourea derivatives serve as highly potent and isozyme selective activators for the recombinant form of human histone deacetylase-8 in the assay system containing Fluor-de-Lys as a fluorescent substrate. The experimental data reveals that such activating feature is manifested via decrease in the K(m) value of the enzyme's substrate and increase in the catalytic turnover rate of the enzyme.
我们首次报告，某些 N-乙酰硫脲衍生物在含有 Fluor-de-Lys 作为荧光底物的检测系统中，作为高度有效的同工酶选择性激活剂，作用于重组人组蛋白去乙酰化酶-8。实验数据表明，这种激活特性是通过降低酶的底物的 K(m) 值和增加酶的催化周转率来体现的。
