Complete amino acid sequence and structure characterization of the taste-modifying protein, miraculin

J Biol Chem. 1989 Apr 25;264(12):6655-9.

Abstract

The taste-modifying protein, miraculin, has the unusual property of modifying sour taste into sweet taste. The complete amino acid sequence of miraculin purified from miracle fruits by a newly developed method (Theerasilp, S., and Kurihara, Y. (1988) J. Biol. Chem. 263, 11536-11539) was determined by an automatic Edman degradation method. Miraculin was a single polypeptide with 191 amino acid residues. The calculated molecular weight based on the amino acid sequence and the carbohydrate content (13.9%) was 24,600. Asn-42 and Asn-186 were linked N-glycosidically to carbohydrate chains. High homology was found between the amino acid sequences of miraculin and soybean trypsin inhibitor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Carboxypeptidases / metabolism
  • Carboxypeptidases A
  • Chromatography, High Pressure Liquid
  • Glycoproteins / ultrastructure*
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Fragments / analysis
  • Plant Proteins / ultrastructure*
  • Solubility

Substances

  • Glycoproteins
  • Peptide Fragments
  • Plant Proteins
  • miraculin protein, Synsepalum dulcificum
  • Carboxypeptidases
  • Carboxypeptidases A