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タイトル: | Five amino acid residues in cysteine-rich domain of human T1R3 were involved in the response for sweet-tasting protein, thaumatin. |
著者: | Masuda, Tetsuya https://orcid.org/0000-0001-5857-5753 (unconfirmed) Taguchi, Wakana Sano, Ayane Ohta, Keisuke Kitabatake, Naofumi Tani, Fumito https://orcid.org/0000-0002-0356-9214 (unconfirmed) |
著者名の別形: | 桝田, 哲哉 |
キーワード: | Thaumatin Sweet-tasting protein Sweet receptor Cysteine-rich domain |
発行日: | Jul-2013 |
出版者: | Elsevier Masson SAS |
誌名: | Biochimie |
巻: | 95 |
号: | 7 |
開始ページ: | 1502 |
終了ページ: | 1505 |
抄録: | 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. |
著作権等: | © 2013 Elsevier Masson SAS. 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。 This is not the published version. Please cite only the published version. |
URI: | http://hdl.handle.net/2433/175269 |
DOI(出版社版): | 10.1016/j.biochi.2013.01.010 |
PubMed ID: | 23370115 |
出現コレクション: | 学術雑誌掲載論文等 |
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