Kay J, Ryle A P
Biochem J. 1971 Jun;123(1):75-82. doi: 10.1042/bj1230075.
Porcine pepsin C is inactivated rapidly and irreversibly by diazoacetyl-dl-norleucine methyl ester in the presence of cupric ions at pH values above 4.5. The inactivation is specific in that complete inactivation accompanies the incorporation of 1mol of inhibitor residue/mol of enzyme and evidence has been obtained to suggest that the reaction occurs with an active site residue. The site of reaction is the beta-carboxyl group of an aspartic acid residue in the sequence Ile-Val-Asp-Thr. This sequence is identical with the active-site sequence in pepsin and the significance of this in terms of the different activities of the two enzymes is discussed.
在pH值高于4.5且存在铜离子的情况下，重氮乙酰-dl-正亮氨酸甲酯能使猪胃蛋白酶C迅速且不可逆地失活。这种失活具有特异性，即每摩尔酶结合1摩尔抑制剂残基时会完全失活，并且已有证据表明该反应发生在活性位点残基上。反应位点是序列Ile-Val-Asp-Thr中天冬氨酸残基的β-羧基。该序列与胃蛋白酶的活性位点序列相同，并讨论了这在两种酶不同活性方面的意义。
