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Title: Five amino acid residues in cysteine-rich domain of human T1R3 were involved in the response for sweet-tasting protein, thaumatin.
Authors: Masuda, Tetsuya  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0001-5857-5753 (unconfirmed)
Taguchi, Wakana
Sano, Ayane
Ohta, Keisuke
Kitabatake, Naofumi
Tani, Fumito  kyouindb  KAKEN_id
Author's alias: 桝田, 哲哉
Keywords: Thaumatin
Sweet-tasting protein
Sweet receptor
Cysteine-rich domain
Issue Date: Jul-2013
Publisher: Elsevier Masson SAS
Journal title: Biochimie
Volume: 95
Issue: 7
Start page: 1502
End page: 1505
Abstract: Thaumatin, a sweet-tasting plant protein, elicits a sweet taste sensation at 50 nM in humans but not rodents. Although it was shown that the cysteine-rich domain (CRD) of human T1R3 (hT1R3) is important for the response to thaumatin, the amino acid residues within CRD critical for response are still unknown. A comparison of the amino acid sequence (69 amino acid residues) of CRD between hT1R3 and mouse T1R3 (mT1R3) revealed sixteen amino acids that differ. In the present study, we converted each of these sixteen amino acids in hT1R3 to their mouse counterpart and examined the response to thaumatin and sucralose using a cell-based assay. No significant decrease in the response to sucralose was seen among any of the sixteen mutants. However, five mutants (Q504K, A537T, R556P, S559P, and R560K) exhibited a significantly diminished response to thaumatin. The five critical residues involved in the response to thaumatin were dispersed in the CRD of hT1R3 and widely distributed when compared to brazzein. The unique intense sweet-taste of thaumatin might be attributed to the different receptor activation mechanism compared to the small molecule sweetener sucralose.
Rights: © 2013 Elsevier Masson SAS.
This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
URI: http://hdl.handle.net/2433/175269
DOI(Published Version): 10.1016/j.biochi.2013.01.010
PubMed ID: 23370115
Appears in Collections:Journal Articles

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