Human renin inhibition by a diazoacyl reagent: relationship of the enzyme to other proteinases.
Human renin inhibition by a diazoacyl reagent: relationship of the enzyme to other proteinases.
复制标题
重氮酰基试剂对人肾素的抑制：该酶与其他蛋白酶的关系。
DOI：
10.1016/0024-3205(75)90210-6
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发表时间：
1975
期刊：
影响因子：
6.1
通讯作者：
R. I. Gregerman
中科院分区：
文献类型：
--
作者：
M. Mckown;R. I. Gregerman
人肾素在Cu（II）存在下被重氮酰基化合物（重氮乙酰甘氨酸乙酯；N2CHCO-Gly-OEt）灭活。这种失活的机制可能与胃蛋白酶和其他几种蛋白酶的失活机制相同：酶活性部位的天冬氨酸残基的β-羧基发生酯化反应。肾素被重氮酰基试剂抑制，对疏水序列的特异性，以及被胃抑素抑制，都表明肾素与酸性蛋白酶，尤其是胃蛋白酶和组织蛋白酶d有密切的关系。然而，肾素作为一种中性蛋白酶，更适合与其他重氮酰基抑制酶一起分类，而不是根据pH最优。建议将这类酶称为“天冬氨酸蛋白酶”。
Human renin is inactivated by a diazoacyl compound (diazoacetylglycine ethyl ester; N2CHCO-Gly-OEt) in the presence of Cu(II). The mechanism of the inactivation is presumably identical to that which has been determined for pepsin and several other proteinases: esterification of the β-carboxyl of an aspartic acid residue at the active site of the enzyme. Renin's inhibition by the diazoacyl reagent, its specificity toward a hydrophobic sequence, and its inhibition by pepstatin, all suggest a close relationship to the acid proteinases, especially pepsin and cathepsin D. However, renin, a neutral proteinase, would be better classified together with other diazoacyl-inhibited enzymes by active site rather than pH optimum. The term “aspartic proteinase” is suggested for this group of enzymes.