Structural insights into catalytic promiscuity of chalcone synthase from Glycine max (L.) Merr.: Coenzyme A-induced alteration of product specificity

• DOI: 10.1016/j.bbrc.2024.150080
• Publication Date: 2024-05-08T07:09:04Z
• Authors: 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
• Keywords: Chalcone; Coenzyme A

Catalytic promiscuity of enzymes plays a pivotal role in driving the evolution plant specialized metabolism. Chalcone synthase (CHS) catalyzes production 2',4,4',6'-tetrahydroxychalcone (THC), common precursor flavonoids, from p-coumaroyl-coenzyme A (-CoA) and three malonyl-CoA molecules. CHS has promiscuous product specificity, producing significant amount p-coumaroyltriacetic lactone (CTAL) vitro. However, mechanistic aspects this remain to be clarified. Here, we show that specificity soybean (GmCHS1) is altered by CoA, reaction product, which selectively inhibits THC (IC