Flavanone 3β-Hydroxylases from Rice: Key Enzymes for Favonol and Anthocyanin Biosynthesis

  • Kim, Jeong Ho (Department of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University) ;
  • Lee, Yoon Jung (Department of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University) ;
  • Kim, Bong Gyu (Department of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University) ;
  • Lim, Yoongho (Department of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University) ;
  • Ahn, Joong-Hoon (Department of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University)
  • Received : 2007.10.30
  • Accepted : 2007.11.26
  • Published : 2008.04.30


Flavanone $3{\beta}$-hydroxylases (F3H) are key enzymes in the synthesis of flavonol and anthocyanin. In this study, three F3H cDNAs from Oryza sativa (OsF3H-1 ~3) were cloned by RT-PCR and expressed in E. coli as gluthatione S-transferase (GST) fusion proteins. The purified recombinant OsF3Hs used flavanone, naringenin and eriodictyol as substrates. The reaction products with naringen and eriodictyol were determined by nuclear magnetic resonance spectroscopy to be dihydrokaempferol and taxifolin, respectively. OsF3H-1 had the highest enzymatic activity whereas the overall expression of OsF3H-2 was highest in all tissues except seeds. Flavanone $3{\beta}$-hydroxylase could be a useful target for flavonoid metabolic engineering in rice.


Flavanone $3{\beta}$-Hydroxylase;Flavonoid;Oryza sativa


Supported by : Rural Development Administration


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