Yokosawa H, Nishikata M, Ishii S
J Biochem. 1984 Jun;95(6):1819-21. doi: 10.1093/oxfordjournals.jbchem.a134795.
A peptide aldehyde inhibitor possessing prolinal at the carboxyl terminus was designed as an inhibitor of post-proline cleaving enzyme by analogy with peptide aldehyde inhibitors of serine and thiol proteases. N-Benzyloxycarbonyl-valyl-prolinal was found to be a potent inhibitor of post-proline cleaving enzyme from ascidian sperm with a K1 value of 2.4 nM. The presence of the aldehyde portion of the inhibitor, as well as its prolonged incubation with the enzyme, is indispensable for the potent inhibitory activity of the inhibitor. These results indicate that N-benzyloxycarbonyl-valyl-prolinal functions as a transition-state aldehyde inhibitor of post-proline cleaving enzyme.
通过与丝氨酸和硫醇蛋白酶的肽醛抑制剂类比，设计了一种在羧基末端含有脯氨醛的肽醛抑制剂作为脯氨酸后切割酶的抑制剂。发现N-苄氧羰基-缬氨酰-脯氨醛是海鞘精子中脯氨酸后切割酶的有效抑制剂，K1值为2.4 nM。抑制剂醛部分的存在及其与酶的长时间孵育对于抑制剂的有效抑制活性是必不可少的。这些结果表明N-苄氧羰基-缬氨酰-脯氨醛作为脯氨酸后切割酶的过渡态醛抑制剂发挥作用。
