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

  title={Complete amino acid sequence and structure characterization of the taste-modifying protein, miraculin.},
  author={S Theerasilp and Hiroyuki Hitotsuya and Shigeo Nakajo and Kazuyasu Nakaya and Y. Nakamura and Yoshie Kurihara},
  journal={The Journal of biological chemistry},
  volume={264 12},
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… Expand

Paper Mentions

Determination of disulfide array and subunit structure of taste-modifying protein, miraculin.
It was concluded that native miraculin in pure form is a tetramer of the 25 kDa-peptide and native miracleulin in crude state or denatured, non-reduced miraculin onyx-containing peptides isolated by HPLC had the taste-modifying activity. Expand
Cloning and sequencing of a cDNA encoding a taste-modifying protein
Richadella dulcijca (Rd) is a native shrub of tropical West Africa. It yields red berries, called ‘miracle fruit’, that have the unusual property in modifying a sour taste into a sweet taste. ForExpand
Functional expression of miraculin, a taste-modifying protein in Escherichia coli.
It is shown that recombinant miraculin expressed in E. coli has taste-modifying properties as a homodimer, not as a monomer, indicating that glycosylation is not essential for the taste- modifying property. Expand
Cloning, sequence analysis and crystal structure determination of a miraculin-like protein from Murraya koenigii.
Based on the amino acid sequence deduced from both cDNA and genomic DNA, the purification of a 21.4kDa protein with trypsin inhibitory activity from seeds of Murraya koenigii is established to be a miraculin-like protein and provides crystal structure at 2.9A resolution. Expand
The primary structure and characterization of carbohydrate chains of the extracellular glycoprotein proteinase inhibitor from latex of Carica papaya.
The result revealed that the latex protein belongs to an extensively diverse plant protein family that includes inhibitors of serine, cysteine and aspartic proteases, a taste-modifying protein, wound responsive proteins, storage proteins, amylase inhibitors and even an oxidoreductase. Expand
Bulky high-mannose-type N-glycan blocks the taste-modifying activity of miraculin.
A yeast expression system for Miraculin was constructed to accelerate analysis of its structure-function relationships, and it was found that the high-mannose-type N-glycan attached in yeast blocks the taste-modifying activity of rMCL. Expand
Molecular cloning of curculin, a novel taste-modifying protein with a sweet taste.
Northern blot analysis showed that the mRNA for curculin was first detected in Curculigo latifolia fruits at 2 weeks after pollination and remained at a constant level for the following 4 weeks. Expand
Molecular modelling of miraculin: Structural analyses and functional hypotheses.
Molecular dynamics simulations at different pH conditions have indicated that at acidic pH the dimer assumes a widely open conformation, in agreement with the hypotheses coming from other studies. Expand
Cloning and sequencing of a cDNA encoding a taste-modifying protein, miraculin.
A cDNA clone encoding a taste-modifying protein, miraculin (MIR), was isolated and sequenced and showed that the mRNA encoding MIR was already expressed in fruits of Richadella dulcifica at 3 weeks after pollination and was present specifically in the pulp. Expand
Structural and functional analysis of miraculin-like protein from Vitis vinifera.
The results of size-exclusion chromatography and sensory analysis illustrated that vvMLP exists as a monomer in solution with no detectable taste-modifying activity, indicating that the protein can act as a moderate trypsin inhibitor. Expand