Functional characterization of Asp-317 mutant of human renin expressed in COS cells

FEBS Lett. 1988 Mar 28;230(1-2):205-8. doi: 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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alanine
  • Amino Acid Sequence
  • Animals
  • Asparagine*
  • Cell Line
  • Cricetinae
  • DNA, Recombinant
  • Enzyme Precursors / biosynthesis
  • Humans
  • Hydrogen-Ion Concentration
  • Molecular Sequence Data
  • Mutation*
  • Plasmids
  • Renin / biosynthesis
  • Renin / genetics
  • Renin / metabolism*
  • Structure-Activity Relationship
  • Transfection
  • Trypsin / metabolism

Substances

  • DNA, Recombinant
  • Enzyme Precursors
  • Asparagine
  • Trypsin
  • Renin
  • Alanine