蛋白水解酶催化的动力学与机制。牛α-胰蛋白酶和β-胰蛋白酶对合成底物水解动力学的比较。
Kinetics and mechanism of catalysis by proteolytic enzymes. A comparison of the kinetics of hydrolysis of synthetic substrates by bovine alpha- and beta-trypsin.
作者信息
Roberts D V, Elmore D T
出版信息
Biochem J. 1974 Aug;141(2):545-54. doi: 10.1042/bj1410545.
Several esters of the alpha-N-toluene-p-sulphonyl and alpha-N-benzoyl derivatives of S-(3-aminopropyl)-l-cysteine and the methyl ester of S-(4-aminobutyl)-N-toluene-p-sulphonyl-l-cysteine were synthesized. The kinetics of hydrolysis of these and esters of the alpha-N-toluene-p-sulphonyl and alpha-N-benzoyl derivatives of l-arginine, l-lysine, S-(2-aminoethyl)-l-cysteine and esters of gamma-guanidino-l-alpha-toluene-p-sulphonamidobutyric acid and alpha-N-toluene-p-sulphonyl-l-homoarginine by alpha- and beta-trypsin were compared. On the basis of values of the specificity constants (k(cat.)/K(m)), the two enzymes display similar catalytic efficiency towards some substrates. In other cases alpha-trypsin is less efficient than beta-trypsin. It is possible that alpha-trypsin possesses greater molecular flexibility than beta-trypsin.
合成了S-(3-氨丙基)-l-半胱氨酸的α-N-甲苯-对-磺酰基和α-N-苯甲酰基衍生物的几种酯以及S-(4-氨丁基)-N-甲苯-对-磺酰基-l-半胱氨酸甲酯。比较了这些化合物以及l-精氨酸、l-赖氨酸、S-(2-氨乙基)-l-半胱氨酸的α-N-甲苯-对-磺酰基和α-N-苯甲酰基衍生物的酯，γ-胍基-l-α-甲苯-对-磺酰胺丁酸酯和α-N-甲苯-对-磺酰基-l-高精氨酸酯被α-胰蛋白酶和β-胰蛋白酶水解的动力学。根据特异性常数（k(cat.)/K(m)）的值，这两种酶对某些底物表现出相似的催化效率。在其他情况下，α-胰蛋白酶的效率低于β-胰蛋白酶。α-胰蛋白酶可能比β-胰蛋白酶具有更大的分子灵活性。
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