Kasche V, Michaelis G, Wiesemann T
AB Biotechnologie II, TU Hamburg-Harburg, F.R.G.
Biomed Biochim Acta. 1991;50(10-11):S38-43.
The sequence- and stereospecificity of the S1- and S' i-subsites (i = 1-3) of bovine alpha-chymotrypsin and trypsin, proteinase K and penicillin amidase from E. coli and A. viscosus has been determined by hydrolysis and kinetically controlled peptide synthesis using different substrates. The data are compared with results for other serine proteases and the thiol protease papain. The stereospecificities differ by orders of magnitude, decreased when the enzyme was immobilized and were influenced when organic solvent molecules were bound to the enzyme.
通过使用不同底物进行水解和动力学控制的肽合成，已确定了牛α-糜蛋白酶、胰蛋白酶、蛋白酶K以及来自大肠杆菌和粘性放线菌的青霉素酰胺酶的S1和S' i亚位点（i = 1 - 3）的序列特异性和立体特异性。将这些数据与其他丝氨酸蛋白酶和硫醇蛋白酶木瓜蛋白酶的结果进行了比较。立体特异性相差几个数量级，当酶固定化时降低，并且当有机溶剂分子与酶结合时受到影响。
