Functional characterization of Asp‐317 mutant of human renin expressed in COS cells
- 28 March 1988
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 230 (1-2) , 205-208
- https://doi.org/10.1016/0014-5793(88)80672-0
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
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