Yamauchi T, Nagahama M, Hori H, Murakami K
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
FEBS Lett. 1988 Mar 28;230(1-2):205-8. doi: 10.1016/0014-5793(88)80672-0.
Renin is an unique aspartyl (acid) protease with optimal activity at neutral pH. It has been suggested that Ala-317 of human renin contributes to neutral optimum pH of the enzyme [(1984) FEBS Lett. 174, 102-111]. The hypothesis was verified by the characterization of mutant renin in which Ala-317 was replaced with Asp by a site-directed mutagenesis. Wild-type and mutant renins, which were expressed in COS cells, exhibited different pH-activity profiles and optimum pH of the mutant enzyme was lower than that of the wild-type enzyme. This result suggests that Ala-317 of human renin plays an important role in the determination of optimum pH of the enzyme.
肾素是一种独特的天冬氨酰（酸）蛋白酶，在中性pH条件下具有最佳活性。有人提出，人肾素的Ala-317有助于该酶的中性最佳pH值[（1984年）欧洲生物化学学会联合会快报。174, 102 - 111]。通过定点诱变将Ala-317替换为Asp的突变肾素的特性验证了这一假设。在COS细胞中表达的野生型和突变型肾素表现出不同的pH-活性曲线，且突变酶的最佳pH值低于野生型酶。该结果表明，人肾素的Ala-317在确定酶的最佳pH值中起重要作用。
