2-Hydroxyisoflavanone dehydratase is a critical determinant of isoflavone productivity in hairy root cultures of Lotus japonicus

Plant Cell Physiol. 2007 Nov;48(11):1652-7. doi: 10.1093/pcp/pcm125. Epub 2007 Oct 4.

Abstract

Hairy root cultures of a model legume, Lotus japonicus, were established to characterize two heterologous cDNAs encoding enzymes involved in isoflavone biosynthesis, i.e. licorice 2-hydroxyisoflavanone synthase (IFS) and soybean 2-hydroxyisoflavanone dehydratase (HID) catalyzing sequential reactions to yield isoflavones. While the control and the IFS overexpressor did not accumulate detectable isoflavones, the HID overexpressors did accumulate daidzein and genistein, showing that HID is a critical determinant of isoflavone productivity. Production of coumestrol in all the genotypes and isoliquiritigenin/liquiritigenin in IFS + HID-overexpressing lines was also noted. These results provide insight into the regulatory mechanism that controls isoflavonoid biosynthesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cells, Cultured
  • Chromatography, Liquid
  • Cytochrome P-450 Enzyme System / genetics
  • Cytochrome P-450 Enzyme System / metabolism*
  • Gene Expression Regulation, Enzymologic
  • Gene Expression Regulation, Plant
  • Isoflavones / biosynthesis*
  • Isoflavones / chemistry
  • Lotus / cytology
  • Lotus / genetics
  • Lotus / metabolism*
  • Mass Spectrometry
  • Models, Biological
  • Molecular Structure
  • Plant Proteins / genetics
  • Plant Proteins / metabolism*
  • Plant Roots / cytology
  • Plant Roots / genetics
  • Plant Roots / metabolism
  • Reverse Transcriptase Polymerase Chain Reaction

Substances

  • Isoflavones
  • Plant Proteins
  • cytochrome P-450 CYP93C2 (Glycyrrhiza echinata)
  • Cytochrome P-450 Enzyme System