Mel'nikov E E, Tsirul'nikov K B, Rasulova F S, Ginodman L M, Rotanova T V
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Bioorg Khim. 1998 Aug;24(8):638-40.
A new efficient substrate, Suc-Phe-Leu-Phe-SBzl, was proposed for studying the function of the Escherichia coli ATP-dependent Lon protease and its modified forms. The kinetic parameters of hydrolysis of the substrate were determined. The esterase activity of protease Lon was found to be nucleotide-regulated.
提出了一种新的高效底物Suc-Phe-Leu-Phe-SBzl,用于研究大肠杆菌ATP依赖型Lon蛋白酶及其修饰形式的功能。测定了该底物水解的动力学参数。发现蛋白酶Lon的酯酶活性受核苷酸调节。