Cross‐reaction of chalcone synthase and stilbene synthase overexpressed in Escherichia coli

FEBS Letters

Shibuya, Masaaki¹  Suh, Dae-Yeon²  Sankawa, Ushio²  Akiyama, Takumi¹  Ebizuka, Yutaka¹  Kurosaki, Fumiya²  Nishioka, Mizue¹  Yamaguchi, Toshio² 

[1] Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan;Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama, 930-0194, Japan

关键词: Chalcone synthase;    Stilbene synthase;    Bisnoryangonin;    p-Coumaroyltriacetic acid lactone;    Cross-reaction;    CHS;    chalcone synthase;    STS;    stilbene synthase;    BNY;    bisnoryangonin;    CTAL;    p-coumaroyltriacetic acid lactone;    TAL;    triacetic acid lactone;    KPi;    potassium phosphate;    Trx-;    thioredoxin-;   

DOI  :  10.1016/S0014-5793(99)01403-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Chalcone synthase (CHS) and stilbene synthase (STS) are related plant polyketide synthases belonging to the CHS superfamily. CHS and STS catalyze common condensation reactions of p-coumaroyl-CoA and three C₂-units from malonyl-CoA but different cyclization reactions to produce naringenin chalcone and resveratrol, respectively. Using purified Pueraria lobata CHS and Arachis hypogaea STS overexpressed in Escherichia coli, bisnoryangonin (BNY, the derailed lactone after two condensations) and p-coumaroyltriacetic acid lactone (the derailed lactone after three condensations) were detected from the reaction products. More importantly, we found a cross-reaction between CHS and STS, i.e. resveratrol production by CHS (2.7–4.2% of naringenin) and naringenin production by STS (1.4–2.3% of resveratrol), possibly due to the conformational flexibility of their active sites.

【 授权许可】

Unknown