Yumoto N, Mizuta K, Tokushige M, Hayashi R
Physiol Chem Phys. 1982;14(4):391-7.
The active species of aspartase from Escherichia coli is further 3-5 fold activated upon limited proteolysis with trypsin releasing carboxy-terminal peptides as reported previously (N. Yumoto, M. Tokushige, and R. Hayashi. Biochim. Biophys. Acta, 616, 319 (1980) ). Survey of the protease specificity for the activation revealed that subtilisin BPN' and several other proteases having far broader substrate specificity than trypsin also activated the enzyme. The results of sequence analyses revealed that subtilisin BPN' cleaved mainly the serylarginine bond near the carboxy-terminal and released an octapeptide, while trypsin cleaved mainly the arginyltyrosine bond which is just next to the subtilisin cleavage site. These results suggest that the protease-mediated activation does not necessarily require a site-specific peptidyl cleavage, but the cleavage of any bond within a certain region centered at arginine, the eighth residue from the carboxy-terminal, is sufficient.
如先前报道（N. Yumoto、M. Tokushige和R. Hayashi。《生物化学与生物物理学报》，616, 319 (1980)），用胰蛋白酶进行有限的蛋白水解，释放出羧基末端肽段后，来自大肠杆菌的天冬氨酸酶的活性形式会进一步被激活3至5倍。对激活该酶的蛋白酶特异性的研究表明，枯草杆菌蛋白酶BPN'和其他几种底物特异性比胰蛋白酶宽泛得多的蛋白酶也能激活该酶。序列分析结果显示，枯草杆菌蛋白酶BPN'主要切割羧基末端附近的丝氨酰精氨酸键，释放出一个八肽，而胰蛋白酶主要切割紧邻枯草杆菌蛋白酶切割位点的精氨酰酪氨酸键。这些结果表明，蛋白酶介导的激活不一定需要位点特异性的肽键切割，但是在以精氨酸（羧基末端第八个残基）为中心的特定区域内切割任何键就足够了。
