Malonyl-coenzyme A:isoflavone 7-O-glucoside-6"-O-malonyltransferase from roots of chick pea (Cicer arietinum L.)

Arch Biochem Biophys. 1984 Nov 1;234(2):513-21. doi: 10.1016/0003-9861(84)90298-4.


A malonyltransferase which catalyzes the malonylation of isoflavone 7-O-glucosides in position 6 of the glucose moiety using malonyl-coenzyme A as acyl donor has been purified 157-fold from 4-day-old roots of chick pea (Cicer arietinum L.). The enzyme showed a pH optimum of 8.0 and a molecular weight of 112,000. The Km for malonylcoenzyme A was 48 microM and, for the chick pea isoflavones biochanin A and formononetin, 36 and 24 microM, respectively. Various other isoflavone, flavone, and flavonol 7-O-glucosides and chalcone 4'-O-glucosides were much poorer substrates. Flavonol 3-O-glucosides and isoflavone 4'-O-glucosides were not malonylated by the malonyltransferase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl Coenzyme A / metabolism
  • Acyltransferases / isolation & purification
  • Acyltransferases / metabolism*
  • Chromatography, High Pressure Liquid
  • Drug Stability
  • Hydrogen-Ion Concentration
  • Kinetics
  • Molecular Weight
  • Plants / enzymology*
  • Substrate Specificity
  • Temperature


  • Acyl Coenzyme A
  • Acyltransferases
  • malonyl-CoA-isoflavone-7-O-glucoside-6''-O-malonyltransferase