Schellenberger V, Braune K, Hofmann H J, Jakubke H D
Sektion Biowissenschaften der Universität Leipzig, Federal Republic of Germany.
Eur J Biochem. 1991 Aug 1;199(3):623-36. doi: 10.1111/j.1432-1033.1991.tb16163.x.
From the literature we collected all available quantitative data on the chymotrypsin-catalyzed hydrolysis of series of amino acid and peptide substrates. Utilizing this data base, we performed calculations on their quantitative structure/activity relationship (QSAR). The substrates were considered to be composed of fragments; log(kcat/Km) values for the substrates resulted from additive contributions of their fragments. Despite the fact that the kinetic constants in the data base were determined by different authors under various reaction conditions, the data are well described by the simple additivity model. Obviously, the intrinsic specificity of chymotrypsin dominates the influence of varying reaction conditions.
我们从文献中收集了所有关于一系列氨基酸和肽底物的胰凝乳蛋白酶催化水解的可用定量数据。利用这个数据库,我们对它们的定量结构/活性关系(QSAR)进行了计算。底物被认为是由片段组成;底物的log(kcat/Km)值来自其片段的加和贡献。尽管数据库中的动力学常数是由不同作者在各种反应条件下测定的,但这些数据可以用简单的加和模型很好地描述。显然,胰凝乳蛋白酶的内在特异性主导了不同反应条件的影响。