Wilk S
Life Sci. 1983 Nov 28;33(22):2149-57. doi: 10.1016/0024-3205(83)90285-0.
Prolyl endopeptidase (E.C. 3.4.21.26) an enzyme previously called post proline cleaving enzyme, TRH-deamidase or kininase B, may play a role in neuropeptide metabolism. This enzyme, highly active in brain and other tissues, catabolizes proline-containing peptides such as substance P, neurotensin, luteinizing hormone-releasing hormone, thyrotropin releasing hormone, bradykinin and angiotensin II. The structure of beta-neo-endorphin suggests that this opioid peptide is formed by the action of prolyl endopeptidase on a precursor of higher molecular weight. Formation of two biologically active fragments of substance P also requires the action of this enzyme. This review summarizes the current knowledge of the biochemistry of this enzyme, and its potential significance for neuropeptide physiology and pharmacology.
脯氨酰内肽酶（E.C. 3.4.21.26）是一种先前被称为前脯氨酸裂解酶、促甲状腺激素释放激素脱酰胺酶或激肽酶B的酶，可能在神经肽代谢中发挥作用。这种酶在大脑和其他组织中具有高活性，可分解含脯氨酸的肽，如P物质、神经降压素、促黄体生成素释放激素、促甲状腺激素释放激素、缓激肽和血管紧张素II。β-新内啡肽的结构表明，这种阿片肽是由脯氨酰内肽酶作用于更高分子量的前体形成的。P物质的两个生物活性片段的形成也需要这种酶的作用。这篇综述总结了关于这种酶的生物化学的当前知识，以及它对神经肽生理学和药理学的潜在意义。
