Nozawa M, Tanizawa K, Kanaoka Y
J Biochem. 1982 Jun;91(6):1837-43. doi: 10.1093/oxfordjournals.jbchem.a133880.
The kinetics of hydrolysis of "inverse substrates," p-amidinophenyl alkanoates, catalyzed by urokinase, plasmin, kallikrein, and trypsins from various sources were studied. Dissociation constants of acyl enzyme-ligand complexes, which are a characteristic parameter of the reaction with "inverse substrates," were analyzed with a view to comparing the spatial requirements of active sites. It was concluded that the spatial restraint of the active site as regards coexistence of the acyl residue and specific ligand is strictest for hog pancreatic kallikrein and this restraint decreases in the following order: human urokinase; bovine plasmin, bovine and hog trypsins; Streptomyces fradiae trypsin; and Streptomyces griseus trypsin.
研究了尿激酶、纤溶酶、激肽释放酶以及来自不同来源的胰蛋白酶催化“反向底物”对脒基苯基链烷酸酯水解的动力学。分析了酰基酶-配体复合物的解离常数，其作为与“反向底物”反应的特征参数，目的是比较活性位点的空间需求。得出的结论是，就酰基残基和特定配体的共存而言，活性位点的空间限制对猪胰激肽释放酶最为严格，且这种限制按以下顺序降低：人尿激酶；牛纤溶酶、牛和猪胰蛋白酶；弗氏链霉菌胰蛋白酶；灰色链霉菌胰蛋白酶。
