Molecular cloning and characterization of a glucosyltransferase catalyzing glucosylation of curcumin in cultured Catharanthus roseus cells

Kaminaga Y., Sahin F. P., Mizukami H.

FEBS Letters, vol.567, no.2-3, pp.197-202, 2004 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 567 Issue: 2-3
  • Publication Date: 2004
  • Doi Number: 10.1016/j.febslet.2004.04.056
  • Journal Name: FEBS Letters
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.197-202
  • Keywords: Catharanthus roseus, CaUGT, Catharanthus roseus UDP-glucosyltransferase, Cell suspension culture, Curcumin, Glucosyltransferase, Heterologous expression, IPTG, isopropyl 1-thio-β-D-galactoside, LS, Linsmaier and Skoog, Substrate specificity
  • Anadolu University Affiliated: No


Catharanthus roseus cell suspension cultures are capable of converting exogenously supplied curcumin to various glucosides. The glucosylation efficiency is enhanced by addition of methyl jasmonate (MJ) to the cultures prior to curcumin administration. Two cDNAs encoding UDP-glucosyltransferases (CaUGT1 and CaUGT2) were isolated from a cDNA library of cultured C. roseus cells, using a PCR method directed at the conserved UDP-binding domain of plant glycosyltransferases. The sequence identity between their deduced amino acid sequences was 27%. The expression of both genes was up-regulated by addition of MJ to the cell cultures although the mRNA level of CaUGT1 was much lower than that of CaUGT2. The corresponding cDNAs were expressed in Escherichia coli as fusion proteins with maltose-binding protein. The recombinant CaUGT1 exhibited no glucosylation activity with either curcumin or curcumin monoglucoside as substrate, whereas the recombinant CaUGT2 catalyzed the formation of curcumin monoglucoside from curcumin and also conversion of curcumin monoglucoside to curcumin diglucoside. The use of the recombinant CaUGT2 may provide a useful new route for the production of curcumin glucosides. © 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.