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Functional characterization of Asp‐317 mutant of human renin expressed in COS cells
Author(s) -
Yamauchi Takeshi,
Nagahama Masami,
Hori Hitoshi,
Murakami Kazuo
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80672-0
Subject(s) - mutant , enzyme , renin–angiotensin system , chemistry , biochemistry , mutagenesis , protease , neutral protease , wild type , enzyme assay , site directed mutagenesis , microbiology and biotechnology , biology , gene , endocrinology , blood pressure
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.