作者:Charles R. Wescott、Alexander M. Klibanov
DOI:10.1021/ja00058a002
日期:1993.3
The substrate specificity of the serine protease subtilisin Carlsberg in the transesterification reaction of N-Ac-L-Ser-OEt and N-Ac-L-Phe-OEt with 1-propanol was examined in 20 anhydrous solvents. The serine substrate was strongly favored in some solvents, while the phenylalanine substrate was greatly preferred in others. A thermodynamic model was derived which correctly predicted the substrate specificity
在 20 种无水溶剂中检测了丝氨酸蛋白酶枯草杆菌蛋白酶在 N-Ac-L-Ser-OEt 和 N-Ac-L-Phe-OEt 与 1-丙醇的酯交换反应中的底物特异性。丝氨酸底物在某些溶剂中非常受欢迎,而苯丙氨酸底物在其他溶剂中非常受欢迎。推导出热力学模型,该模型正确地预测作为底物的溶剂-水分配系数和酶催化的酯在水中水解的底物特异性的函数的底物特异性。该模型独立于底物和底物,只要后者在过渡态从溶剂中除去