Corey M J, Hallakova E, Pugh K, Stewart J M
Department of Biochemistry, University of Colorado School of Medicine, Denver 80262.
Appl Biochem Biotechnol. 1994 May-Jun;47(2-3):199-210; discussion 210-2. doi: 10.1007/BF02787935.
The synthetic peptide Chymohelizyme-1 (CHZ-1) exhibits esterase activity against carbobenzoxytyrosine p-nitrophenyl ester (ZTONP), carbobenzoxyalanine p-nitrophenyl ester (ZAONP), and t-butyloxy-carbonyltyrosine p-nitrophenyl ester (BocTONP). However, earlier reports of catalytic activity against less labile esters and amides have proven to be incorrect. The major reason for the errors appears to have been the omission of certain controls in the previous work. Although the catalytic triad does not appear to be functioning as designed, the catalytic activity of CHZ-1 does depend on the integrity of its primary structure. The pH dependence of hydrolysis of ZTONP points to general-base catalysis, whereas a preference for hydrophobic substrates suggest that the structure of CHZ-1 is performing some other role in assisting catalysis.
合成肽Chymohelizyme-1（CHZ-1）对苄氧羰基酪氨酸对硝基苯酯（ZTONP）、苄氧羰基丙氨酸对硝基苯酯（ZAONP）和叔丁氧羰基酪氨酸对硝基苯酯（BocTONP）表现出酯酶活性。然而，早期关于其对较稳定酯和酰胺的催化活性的报道已被证明是错误的。这些错误的主要原因似乎是之前的研究中遗漏了某些对照。尽管催化三联体似乎并未按设计发挥作用，但CHZ-1的催化活性确实取决于其一级结构的完整性。ZTONP水解的pH依赖性表明存在一般碱催化，而对疏水性底物的偏好表明CHZ-1的结构在辅助催化中发挥着其他作用。
