CYP81E1, a cytochrome P450 cDNA of licorice (Glycyrrhiza echinata L.), encodes isoflavone 2'-hydroxylase

Biochem Biophys Res Commun. 1998 Oct 9;251(1):67-70. doi: 10.1006/bbrc.1998.9414.


The microsome of yeast cells overexpressing CYP81E1, a cytochrome P450 cDNA recently cloned from licorice (Glycyrrhiza echinata L., Fabaceae), catalyzed the hydroxylation of isoflavones, daidzein and formononetin, to yield 2'-hydroxyisoflavones, 2'-hydroxydaidzein, and 2'-hydroxyformononetin, respectively. The chemical structures of the reaction products were confirmed by mass spectrometric analysis. Genistein also yielded a putative 2'-hydroxylated product, but flavanones and cinnamic acid derivatives were not used as substrates for the reaction with the recombinant yeast microsome. CYP81E1 protein was thus demonstrated for the first time to be isoflavone 2'-hydroxylase involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cloning, Molecular
  • Cytochrome P-450 Enzyme System / genetics*
  • Genes, Plant / genetics
  • Glycyrrhiza / enzymology*
  • Glycyrrhiza / genetics*
  • Isoflavones / metabolism
  • Mixed Function Oxygenases / genetics*
  • Models, Molecular
  • Molecular Sequence Data
  • Plants, Medicinal*


  • Isoflavones
  • Cytochrome P-450 Enzyme System
  • Mixed Function Oxygenases
  • cytochrome P-450 CYP81E1 (Glycyrrhiza echinata)

Associated data

  • GENBANK/AB001379