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Updated: Oct 4, 2025

Identifying Amino Acid Overproducers Using Rare-Codon-Rich Markers
Published on: June 24, 2019
Replacing arginine 99 with leucine to study the kinetics of interconnected allosteric interactions between FFAR4 and
Bo Niu1, Dingqiang Lu2, Ziqing Zheng1
1College of Biotechnology & Food Science, Tianjin University of Commerce, Tianjin, China.
Abstract:
The long-chain fatty acid receptor FFAR4 is the main G-protein-coupled receptor in the body for detecting long-chain fatty acids. It has been shown that Arg99 may be an important residue for fatty acid recognition and for the activation of hFFAR4, though direct evidence is still lacking. In this study, Arg99 on hFFAR4 was substituted with leucine by genetic manipulation, and a double-layer gold nanoparticle biosensor based on hFFAR4 (Arg99 → Leu) was constructed. The interconnected allosteric interaction between 11 naturally occurring fatty acid ligands and the receptor was determined. The results showed that Arg99 is the key residue on hFFAR4 for the recognition of the carboxyl group on fatty acids. This study offered direct quantitative evidence for the role played by different residues in receptor-ligand recognition and interconnected allosterism, providing a new approach for investigating the mechanisms and kinetics of interconnected receptor-ligand allosterism.
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