Inosine-5'-monophosphate interacts with the TAS1R3 subunit to enhance sweet taste detection.

ABSTRACT: Umami and sweet taste detection is mediated by the activation of the TAS1R1/TAS1R3 and TAS1R2/TAS1R3 receptors, respectively. TAS1R2-Venus flytrap domain (VFT) constitutes the primary ligand-binding site for most of the sweeteners whereas TAS1R1-VFT contains the orthosteric binding site for umami compounds. Inosine-5'-monophosphate (IMP), previously known to potentiate umami taste, binds to a site of TAS1R1-VFT adjacent to the L-glutamate site leading to umami synergy. However, the involvement of the TAS1R3 subunit in umami receptor-ligand interactions or in synergy with IMP has never been demonstrated. To elucidate the VFT contribution to umami and sweet detection, we expressed human TAS1R1- and TAS1R3-VFTs in bacteria. Ligand binding studies quantified by intrinsic tryptophan fluorescenc

SUBMITTER: Belloir C 

PROVIDER: S-EPMC11872639 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature