Riechmann L, Kasche V
Biochem Biophys Res Commun. 1984 Apr 30;120(2):686-91. doi: 10.1016/0006-291x(84)91310-x.
The mechanism of peptide semisynthesis catalyzed by alpha-chymotrypsin and beta-trypsin has been investigated. The dependence of the apparent ratio of the second order rate constants for the deacylation of the acyl-enzyme intermediate by water and other nucleophiles (amino acid amides) on the nucleophile concentration indicates a mechanism that involves two acyl-enzymes. One with and one without bound nucleophile that both can be deacylated by water. The nucleophile specificity in peptide semisynthesis catalyzed by the proteases was found to reflect the P1-specificity in the corresponding hydrolytic reaction.
已经研究了α-胰凝乳蛋白酶和β-胰蛋白酶催化的肽半合成机制。水和其他亲核试剂（氨基酸酰胺）对酰基酶中间体脱酰作用的二级速率常数的表观比率对亲核试剂浓度的依赖性表明，该机制涉及两种酰基酶。一种结合了亲核试剂，另一种没有结合亲核试剂，两者都可以被水脱酰。发现蛋白酶催化的肽半合成中的亲核试剂特异性反映了相应水解反应中的P1特异性。
