Membrane bound pituitary metalloendopeptidase: apparent identity to enkephalinase.
Membrane bound pituitary metalloendopeptidase: apparent identity to enkephalinase.
复制标题
膜结合垂体金属内肽酶：与脑啡肽酶明显相同。
DOI：
10.1016/0006-291x(81)91508-4
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发表时间：
1981
影响因子：
3.1
通讯作者：
Orlowski,M
中科院分区：
文献类型：
--
作者：
Almenoff,J;Wilk,S;Orlowski,M
来自牛垂体的锌-金属内肽酶对疏水氨基酸氨基侧的键具有特异性，在Gly-Phe键上切割Met-和亮氨酸脑啡肽，分别释放出ph -Met和ph -亮氨酸。这种酶还能水解催产素、缓激肽、神经紧张素和几种合成底物中疏水氨基酸的氨基侧键。二肽c端水解键上的游离羧基不是活性的必要条件。这种酶也存在于脑膜中。这种酶在大脑中的区域分布、对天然和合成底物的特异性以及对抑制剂的敏感性表明，这种酶与一种被称为“脑啡肽酶”的活性相同，这种酶被描述为二肽基羧肽酶。数据表明，该酶是一种内肽酶，具有类似于一组微生物蛋白酶的特异性，其中一种是热溶酶。
A membrane bound zinc-metalloendopeptidase from bovine pituitaries with a specificity toward bonds on the amino side of hydrophobic amino acids, cleaves Met- and Leu-enkephalin at the Gly-Phe bond, releasing Phe-Met and Phe-Leu respectively. The enzyme also hydrolyzes bonds on the amino side of hydrophobic amino acids in oxytocin, bradykinin, neurotensin and several synthetic substrates. A free carboxyl group on a dipeptide C-terminal to the hydrolyzed bond is not a requirement for activity. The enzyme is also present in brain membrane fractions. The regional distribution of this enzyme in brain, its specificity toward natural and synthetic substrates, and its sensitivity to inhibitors, suggest that the enzyme is identical to an activity referred to as “enkephalinase”, which has been described as dipeptidyl carboxypeptidase. The data show that the enzyme is an endopeptidase with a specificity similar to that of a group of microbial proteases, one of which is thermolysin.