Further characterization and regulation of malonyl-coenzyme A: flavonoid glucoside malonyltransferases from parsley cell suspension cultures

Arch Biochem Biophys. 1983 Oct 1;226(1):206-17. doi: 10.1016/0003-9861(83)90286-2.


Two malonyltransferases, malonyl-CoA:flavone/flavonol 7-O-glucoside malonyltransferase and malonyl-CoA:flavonol 3-O-glucoside malonyltransferase, were purified to apparent homogeneity from uv-irradiated parsley cell cultures. Both purified enzymes appear to be specific for flavonoid glycosides. Additional malonyltransferases, active toward several phenol glucosides other than flavonoids, were present in partially purified 7-O-glucoside malonyltransferase preparations. Antibodies raised against the purified 3-O-glucoside malonyltransferase did not inhibit the activity of the 7-O-glucoside malonyltransferase over a wide antibody concentration range. Determination of the rate of synthesis in vivo of the 3-O-glucoside malonyltransferase after ultraviolet light-pulse induction of parsley cells revealed two maxima at 6 and 30 h, respectively. These results indicate that the induced changes in 3-O-glucoside malonyltransferase activity were the consequence of either a repeated change in the rate of synthesis of one enzyme species or changes in the synthesis rates of more than one enzyme species.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyltransferases / isolation & purification
  • Acyltransferases / metabolism*
  • Cells, Cultured
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Molecular Weight
  • Plants / enzymology*
  • Plants / radiation effects
  • Substrate Specificity


  • Acyltransferases
  • malonyl-CoA-flavone-flavonol-7-O-glycoside malonyltransferase