Kuriavyĭ V V, Usacheva A M, Bruskov V I
Mol Biol (Mosk). 1989 May-Jun;23(3):822-9.
Detailed analysis of the kinetics of inhibition of E. coli RNA-polymerase-catalyzed synthesis of dinucleotide pppApU by 8-oxy-GTP and 8-Br-GTP on promoter A1 of the bacteriophage T7 delta D111 with an incomplete set of substrates was carried out. In accordance with the mathematical models obtained, we calculated quantitative parameters of binding of these nucleotide analogs to the centers whose geometry is suitable for incorporation of ATP and UTP. 8-oxy-GTP and 8-Br-GTP compete with ATP for the binding center (their steady-state dissociation constant ratios are 2.1 and 2.4, respectively, whereas the constant for ATP is 0.3 mM) but, unlike ATP, they are not incorporated into the product. 8-oxy-GTP competes also with UTP (its steady-state dissociation constant ratio is 21.6, the constant for UTP is 0.03 mM). 8-Br-GTP does not interact with the binding center of UTP.
对8-氧代-GTP和8-溴-GTP在底物不完全的情况下对噬菌体T7δD111启动子A1上大肠杆菌RNA聚合酶催化合成二核苷酸pppApU的抑制动力学进行了详细分析。根据所得数学模型，我们计算了这些核苷酸类似物与几何结构适合ATP和UTP掺入的中心结合的定量参数。8-氧代-GTP和8-溴-GTP与ATP竞争结合中心（它们的稳态解离常数比分别为2.1和2.4，而ATP的常数为0.3 mM），但与ATP不同的是，它们不掺入产物中。8-氧代-GTP也与UTP竞争（其稳态解离常数比为21.6，UTP的常数为0.03 mM）。8-溴-GTP不与UTP的结合中心相互作用。
