Stein R L
Arch Biochem Biophys. 1985 Feb 1;236(2):677-80. doi: 10.1016/0003-9861(85)90673-3.
Steady-state kinetic parameters were determined at pH 7.4 and 25 degrees C for the human leukocyte elastase-catalyzed hydrolysis of several N-carbobenzoxy-L-amino acid p-nitrophenyl esters. The substrate specificity for these esters was quite broad, and included the Gly, Phe, and Tyr derivatives. Together with reports of a much narrower P-1 specificity for peptide-based substrates, these results suggest that interactions remote from the scissle bond between enzyme and substrate regulate primary specificity. Also, it was found that kc and kc/Km did not exhibit the same dependence on substrate structure. This is interpreted to suggest that there are significant differences in P-1 specificity between acylation and deacylation for leukocyte elastase-catalyzed reactions.
在pH 7.4和25℃条件下，测定了人白细胞弹性蛋白酶催化几种N-苄氧羰基-L-氨基酸对硝基苯酯水解的稳态动力学参数。这些酯的底物特异性相当广泛，包括甘氨酸、苯丙氨酸和酪氨酸衍生物。结合关于肽基底物的P-1特异性要窄得多的报道，这些结果表明，酶与底物之间远离裂解键的相互作用调节了一级特异性。此外，还发现kc和kc/Km对底物结构的依赖性并不相同。这被解释为表明在白细胞弹性蛋白酶催化反应的酰化和脱酰化过程中，P-1特异性存在显著差异。
