Brooks R R, Andersen J A
Biochem J. 1978 Jun 1;171(3):725-32. doi: 10.1042/bj1710725.
Two reactions of bacteriophage-Qbeta RNA polymerase with synthetic templates were characterized and used to study the effects of substrate, metal and template on inhibition by Pi and PPi. Analysis of the poly(C)-dependent reaction yielded results on kinetics, GTP-dependence, preference for Mn2+ over Mg2+, and Michaelis constants for template similar to those in the literature. New data are provided for the poly(U2,C)-dependent reaction. Our results suggest that GTP and Mn2+ can form relatively stable complexes with the polymerase and that such complexes change the interaction of the enzyme with the inhibitors, Pi and PPi.
对噬菌体-Qβ RNA聚合酶与合成模板的两种反应进行了表征,并用于研究底物、金属和模板对Pi和PPi抑制作用的影响。对依赖于聚(C)的反应进行分析,得出了有关动力学、GTP依赖性、对Mn2+比对Mg2+的偏好性以及模板的米氏常数等结果,这些结果与文献中的结果相似。提供了关于依赖于聚(U2,C)的反应的新数据。我们的结果表明,GTP和Mn2+可以与聚合酶形成相对稳定的复合物,并且这种复合物会改变酶与抑制剂Pi和PPi的相互作用。