Liacouras A S, Anderson E P
Mol Cell Biochem. 1977 Oct 7;17(3):141-6. doi: 10.1007/BF01730833.
The combined phosphorylation of uridine and cytidine by a partially purified preparation of uridine-cytidine kinase has been studied with dual-substrate kinetics. The kinetic patterns obtained are consistent with the theoretical analysis for two competing, alternate substrates interacting with a single enzyme. Thus, despite feedback regulation of the kinase by both UTP and CTP, the results allow a clear conclusion that both nucleosides are phosphorylated by the same enzyme, and probably at a single site, rather than by two closely related isozymes, each specific for one pyrimidine.
利用双底物动力学研究了部分纯化的尿苷 - 胞苷激酶制剂对尿苷和胞苷的联合磷酸化作用。所获得的动力学模式与两种竞争性替代底物与单一酶相互作用的理论分析一致。因此,尽管该激酶受到UTP和CTP的反馈调节,但结果仍可明确得出结论:两种核苷均由同一种酶磷酸化,且可能在单个位点,而非由两种密切相关的同工酶分别特异性催化一种嘧啶。