Complete amino acid sequence and structure characterization of the taste-modifying protein, miraculin.
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.
Theerasilp
S
S
Department of Chemistry, Faculty of Education, Yokohama National University, Japan.
Hitotsuya
H
H
Nakajo
S
S
Nakaya
K
K
Nakamura
Y
Y
Kurihara
Y
Y
D000595:Amino Acid Sequence; D002268:Carboxypeptidases / Q000378:metabolism; D043422:Carboxypeptidases A; D002851:Chromatography, High Pressure Liquid; D006023:Glycoproteins / Q000648:ultrastructure*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D010940:Plant Proteins / Q000648:ultrastructure*; D012995:Solubility
D006023:Glycoproteins; D010446:Peptide Fragments; D010940:Plant Proteins; C008533:miraculin protein, Synsepalum dulcificum; D002268:Carboxypeptidases; D043422:Carboxypeptidases A