Site-directed mutagenesis of human prorenin. Substitution of three arginine residues in the propeptide with glutamine residues yields active prorenin.

doi:10.1093/oxfordjournals.jbchem.a123005

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Article

Site-directed mutagenesis of human prorenin. Substitution of three arginine residues in the propeptide with glutamine residues yields active prorenin.

Journal of biochemistry - 1 Jan 1990

Yamauchi T, Nagahama M, Watanabe T, Ishizuka Y, Hori H, Murakami K

Abstract excerpt

Human prorenin is an inactive zymogen comprising 43 amino acid residues at the amino terminus of human renin. The aim of this work was to determine why prorenin is inactive at neutral pH. Eighteen different mutant prorenins, in which positively charged residues in the propeptide were substituted with either glutamine (Gln) or lysine (Lys) residues by site-directed mutagenesis, were expressed in COS-7 cells and...

Topics

Amino Acid Sequence
Animals
Arginine
Aspartic Acid Endopeptidases
Base Sequence
Cattle
Cell Line
Endopeptidases
Enzyme Precursors
Glutamine
Humans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Hydrogen-Ion Concentration

Mice

Molecular Sequence Data

Mutation

Precipitin Tests

Protein Engineering

Rats

Source

Open in PubMed

Identifiers

PMID: 2185237
DOI: 10.1093/oxfordjournals.jbchem.a123005

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2185237-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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