Highly Probable Active Site of the Sweet Protein Monellin
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概要
- 論文の詳細を見る
The sweet protein monellin consists of two noncovalently associated polypeptide chains, the A chain of 44 amino acid residues and B chain of 50 residues. Synthetic monellin is 4000 times as sweet as sucrose on a weight basis, and the native conformation is essential for the sweet taste. Knowledge of the active site of monellin will provide important information on the mode of interaction between sweeteners and their receptors. If the replacement of a certain amino acid residue in monellin removes the sweet taste, while the native conformation is retained, it may be concluded that the position replaced is the active site. Our previous replacement studies on Asp residues in the A chain did not remove the sweet taste. The B chain contains two Asp residues at positions 7 and 21,which were replaced by Asn. [Asn^<B21>] Monellin and [Asn^<B7>] monellin were 7000 and 20 times sweeter than sucrose, respectively. The low potency of the [Asn^<B7>] monellin indicates that Asp^<B7> participates in binding with the receptor. Asp^<B7>was then replaced by Abu. [Abu^<B7>] Monellin was devoid of sweetness, and retained the native conformation. Asp^<B7> is located at the surface of the molecule (Ogata et al.). These results suggest that Asp^7 in the B chain is the highly probable active site of monellin.
- 社団法人日本農芸化学会の論文
- 1992-12-23
著者
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Nio Noriki
Central Research Laboratories, Ajinomoto Co., Inc.
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Ariyoshi Yasuo
Central Research Laboratories, Ajinomoto Co., Inc.
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Nio N
Ajinomoto Co. Inc. Kanagawa Jpn
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Ariyoshi Y
Ajinomoto Co. Inc. Kawasaki Jpn
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Ariyoshi Yasuo
Central Research Laboratories Ajinomoto Co. Inc
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Kohmura M
Ajinomoto Co. Inc. Kawasaki Jpn
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Kohmura Masanori
Central Research Laboratories, Ajinomoto Co., Inc.
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Kohmura Masanori
Central Research Laboratories Ajinomoto Co. Inc.
関連論文
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- Immobilization of Enzyme in Protein Films Prepared Using Transglutaminase(Food & Nutrition)
- α_-Casein Film Prepared Using Transglutaminase(Food & Nutrition)
- Solid-phase Synthesis and Structure-Taste Relationships of Analogs of the Sweet Protein Monellin
- Highly Probable Active Site of the Sweet Protein Monellin
- Solid-Phase Synthesis of [Asn^]-, [Asn^]-, [Gln^]-, and [Asn^]Monellin, Analogues of the Sweet Protein Monellin
- Solid-Phase Synthesis of Crystalline [Ser^] B-Chain Monellin, an Analogue of the Sweet Protein Monellin(Organic Chemistry)
- Solid-Phase Synthesis of Crystalline Monellin, a Sweet Protein(Organic Chemistry)
- Solid-Phase Synthesis and Crystallization of [Asn^, Gln^, Asn^]-A-Chain-[Asn^, Glu^]-B-Chain-Monellin, an Analogue of the Sweet Protein Monellin(Organic Chemistry)
- Complete Amino Acid Sequence of the Sweet Protein Monellin(Biological Chemistry)
- Solid-Phase Synthesis and Crystallization of Monellin, an Intensely Sweet Protein(Organic Chemistry)
- Inhibition of Angiotensin-Converting Enzyme by Synthetic Peptide Fragments of Various β-Caseins(Biological Chemistry)
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- Functional Properties of Heterologous Polymer Prepared by Transglutaminase between Milk Casein and Soybean Globulin(Food & Nutrition)
- Glutamine-specific Deamidation of α_-Casein by Transglutaminase(Food & Nutrition)
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- Functional Properties of Food Proteins Polymerized by Transglutaminase
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- The Reaction of Aspartyl Dipeptide Esters with Ketones
- Studies of Hydroxy Amino Acids. II. The Separation of Diastereoisomers of Hydroxy Amino Acids
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- Structure-taste relationships of aspartyl tetrapeptide esters.