Cloning and Characterization of a cDNA Encoding Beta-Amyrin Synthase Involved in Glycyrrhizin and Soyasaponin Biosyntheses in Licorice

Biol Pharm Bull. 2001 Aug;24(8):912-6. doi: 10.1248/bpb.24.912.

Abstract

An oxidosqualene cyclase cDNA, termed GgbAS1, was isolated from cultured cells of licorice (Glycyrrhiza glabra) by heterologous hybridization with cDNA of Arabidopsis thaliana LUP1 lupeol synthase. The yeast transformed with an expression vector containing the open reading frame of GgbAS1 produced beta-amyrin, indicating that GgbAS1 encodes beta-amyrin synthase involved in the glycyrrhizin and soyasaponin biosyntheses in licorice. Northern blot analysis showed that the level of beta-amyrin synthase mRNA was drastically changed in the cultured licorice cells, whereas the mRNA level of cycloartenol synthase was relatively constant.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Blotting, Northern
  • Blotting, Southern
  • Cells, Cultured
  • Cloning, Molecular
  • DNA, Complementary / biosynthesis*
  • DNA, Complementary / genetics
  • Glycyrrhiza / metabolism*
  • Glycyrrhizic Acid / metabolism*
  • Intramolecular Transferases / biosynthesis*
  • Intramolecular Transferases / genetics
  • Intramolecular Transferases / metabolism
  • Molecular Sequence Data
  • Oleanolic Acid* / analogs & derivatives*
  • RNA, Messenger / biosynthesis
  • RNA, Messenger / genetics
  • Saccharomyces cerevisiae / metabolism
  • Saponins / biosynthesis*

Substances

  • DNA, Complementary
  • RNA, Messenger
  • Saponins
  • soyasaponin I
  • Glycyrrhizic Acid
  • Oleanolic Acid
  • Intramolecular Transferases
  • 2,3-oxidosqualene-beta-amyrin-cyclase
  • cycloartenol synthase