Kuznetsov Aleksei, Uri Asko, Raidaru Gerda, Järv Jaak
Institute of Organic and Bioorganic Chemistry, University of Tartu, 2 Jakobi Str, 51014, Estonia.
Bioorg Chem. 2004 Dec;32(6):527-35. doi: 10.1016/j.bioorg.2004.05.004.
Kinetic analysis of the inhibition of the phosphorylation of Kemptide, (LRRASLG), catalyzed by the catalytic subunit of cAMP-dependent protein kinase, by a peptide-nucleoside conjugate inhibitor AdcAhxArg6 was carried out over a wide range of ATP and peptide concentrations. A simple procedure was proposed for characterization of the interaction of this inhibitor with the free enzyme, and with the enzyme-ATP and enzyme-peptide complexes. The second-order rate constants, calculated from the steady-state reaction kinetics, were used for this analysis to avoid the complications related to the complex catalytic mechanism of the protein kinase catalyzed reaction.
在广泛的ATP和肽浓度范围内，对肽 - 核苷共轭抑制剂AdcAhxArg6抑制由环磷酸腺苷依赖性蛋白激酶催化亚基催化的Kemptide（LRRASLG）磷酸化进行了动力学分析。提出了一种简单的程序来表征该抑制剂与游离酶、酶 - ATP复合物和酶 - 肽复合物之间的相互作用。从稳态反应动力学计算得到的二级速率常数用于该分析，以避免与蛋白激酶催化反应复杂催化机制相关的复杂性。
