Tanizawa K, Yamada H, Kanaoka Y
Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Biochim Biophys Acta. 1987 Nov 26;916(2):205-12. doi: 10.1016/0167-4838(87)90110-5.
Trypsin-specific substrate analogs, 'inverse substrates', carrying chiral acyl group were synthesized. Kinetic analysis of the trypsin-catalyzed hydrolysis of these substrates revealed that the deacylation process is also appropriate for discrimination between enantiomers. The enantiomeric preference during the deacylation process was analyzed by comparing the hydrolytic rates corresponding to eight enantiomeric pairs of the substrates. The spatial requirement of the enzyme active site for catalytic efficiency is discussed, based on the steric characteristics of the optically active acyl residues.
合成了带有手性酰基的胰蛋白酶特异性底物类似物，即“反向底物”。对这些底物的胰蛋白酶催化水解进行动力学分析表明，脱酰基过程也适用于对映体的区分。通过比较对应于底物的八对对映体的水解速率，分析了脱酰基过程中的对映体偏好。基于旋光性酰基残基的空间特征，讨论了酶活性位点对催化效率的空间要求。
