Pufferfish taste receptor more versatile than a human's, detecting both savory L- and sweet D-amino acids
Our sense of taste is critical for survival, alerting us to substances that provide vital nutrients and those that might poison us. Now, a team led by researchers from the University of Osaka has discovered how one such taste receptor in pufferfish can detect a surprisingly wide range of flavors at once. Their study is published in the Proceedings of the National Academy of Sciences.
A recent study published in the Proceedings of the National Academy of Sciences has revealed that a pufferfish taste receptor is more versatile than the human umami receptor. This receptor, found in pufferfish, detects a wider range of amino acids, including both L- and D-forms, unlike the human umami receptor which primarily detects L-amino acids.
Researchers from the University of Osaka discovered the 3D crystal structure of Tas1r1/Tas1r3, a protein that functions similarly to the human umami receptor. The pufferfish receptor's ability to bind both L- and D-amino acids is believed to be driven by its diet, which consists of mollusks and crustaceans rich in D-amino acids.
The study identified unique molecular interactions that enable the receptor to maintain closure even when the fit is imperfect, allowing it to detect a broader range of amino acids. This discovery provides insights into taste perception and may aid in the development of new umami flavors for humans, livestock, and fisheries.
Written by urgent.news from Phys.org's reporting — not their text. Machine-written — may contain errors; check the original before relying on it.
