Toshiyuki Waki, Riki Imaizumi, Kaichi Uno, Yamato Doi, Misato Tsunashima, Sayumi Yamada, Ryo Mameda, Shun Nakata, Taro Yanai, Kohei Takeshita, Naoki Sakai, Kunishige Kataoka, Masaki Yamamoto, Seiji Takahashi, Toru Nakayama, Satoshi Yamashita
Catalytic promiscuity of enzymes plays a pivotal role in driving the evolution of plant specialized metabolism. Chalcone synthase (CHS) catalyzes the production of 2',4,4',6'-tetrahydroxychalcone (THC), a common precursor of plant flavonoids, from p-coumaroyl-coenzyme A (-CoA) and three malonyl-CoA molecules. CHS has promiscuous product specificity, producing a significant amount of p-coumaroyltriacetic lactone (CTAL) in vitro. However, mechanistic aspects of this CHS promiscuity remain to be clarified. Here, we show that the product specificity of soybean CHS (GmCHS1) is altered by CoA, a reaction product, which selectively inhibits THC production (IC50 , 67 μM) and enhances CTAL production...
May 8, 2024: Biochemical and Biophysical Research Communications