Cloning and functional expression in Escherichia coli of a cDNA encoding cardenolide 16'-O-glucohydrolase from Digitalis lanata Ehrh

Plant Cell Physiol. 2000 Nov;41(11):1293-8. doi: 10.1093/pcp/pcd060.

Abstract

A clone of cardenolide 16'-O-glucohydrolase cDNA (CGH I) was obtained from Digitalis lanata which encodes a protein of 642 amino acids (calculated molecular mass 73.2 kDa). The amino acid sequence derived from CGH I showed high homology to a widely distributed family of beta-glucohydrolases (glycosyl hydrolases family 1). The recombinant CGH I protein produced in Escherichia coli had CGH I activity. CGH I mRNA was detected in leaves, flowers, stems and fruits of D. lanata.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Blotting, Northern
  • Cardenolides / metabolism
  • Cloning, Molecular
  • DNA, Complementary / chemistry
  • DNA, Complementary / genetics*
  • Digitalis / enzymology
  • Digitalis / genetics*
  • Escherichia coli / genetics*
  • Gene Expression Regulation, Enzymologic
  • Glucosidases / genetics*
  • Glucosidases / metabolism
  • Molecular Sequence Data
  • Plant Proteins*
  • Plants, Medicinal*
  • Plants, Toxic*
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Sequence Alignment
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Tissue Distribution

Substances

  • Cardenolides
  • DNA, Complementary
  • Plant Proteins
  • RNA, Messenger
  • Cardenolide 16-O-glucohydrolase, Digitalis lanata
  • Glucosidases