Functional characterization of Asp-317 mutant of human renin expressed in COS cells |
| |
| Authors: | T Yamauchi M Nagahama H Hori K Murakami |
| |
| Affiliation: | Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan. |
| |
| Abstract: | 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. |
| |
| Keywords: | Renin Protein engineering Optimum pH Mutant expression (COS cell, Human) |
| 本文献已被 ScienceDirect 等数据库收录！ |
