Angiotensinogen cleavage by renin: importance of a structurally constrained N-terminus
Angiotensinogen cleavage by renin: importance of a structurally constrained N-terminus
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DOI：
10.1016/s0014-5793(98)01145-4
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发表时间：
1998-10-02
期刊：
影响因子：
3.5
通讯作者：
Coughlin, PB
中科院分区：
文献类型：
--
作者：
Streatfeild-James, RMA;Williamson, D;Coughlin, PB
血管紧张素原是一种血浆丝氨酸，作为十肽血管紧张素I的供体，它被肾素从N端切割下来。为了评价丝氨酸骨架对肽切割的贡献，我们制备了携带血管紧张素原N端的α(1)-抗胰蛋白酶嵌合分子，并测定了血管紧张素I释放的动力学参数，血浆血管紧张素原的K-m比手性蛋白低18倍，催化效率高4倍。我们还证明了Cys-18参与了一个二硫键，并提出了对N末端的限制深刻地影响了与肾素的相互作用。(C)1998年欧洲生化学会联合会。
Angiotensinogen, a plasma serpin, functions as a donor of the decapeptide angiotensin I, which is cleaved from the N-terminus by renin, To assess the contribution of the serpin framework to peptide cleavage we produced a chimaeric molecule of alpha(1)-antitrypsin carrying the angiotensinogen N-terminus and determined the kinetic parameters for angiotensin I release, The K-m for plasma angiotensinogen was 18-fold lower than for the chiroaeric protein while the catalytic efficiency was four-fold higher. We also show that Cys-18 participates in a disulphide bond and propose that constraints on the N-terminus profoundly affect the interaction with renin. (C) 1998 Federation of European Biochemical Societies.