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PMID: 2708331 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

The Journal of biological chemistry ·Vol. 264 ·No. 12 ·1989-04-25 ·Pages 6655-9

Theerasilp S, Hitotsuya H, Nakajo S, Nakaya K, Nakamura Y, Kurihara Y

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.

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
Chemicals
Glycoproteins Peptide Fragments Plant Proteins miraculin protein, Synsepalum dulcificum Carboxypeptidases Carboxypeptidases A
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Theerasilp S
Department of Chemistry, Faculty of Education, Yokohama National University, Japan.
Hitotsuya H
Nakajo S
Nakaya K
Nakamura Y
Kurihara Y
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1989-04-25
Pages
6655-9
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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