Molecular characterization of flavonoid malonyltransferase from Oryza sativa

Plant Physiol Biochem. Nov-Dec 2009;47(11-12):991-7. doi: 10.1016/j.plaphy.2009.08.004. Epub 2009 Aug 27.


In this study, a flavonoid malonyltransferase (OsMaT-2) was cloned from Oryza sativa, and the recombinant protein OsMaT-2 was purified via affinity chromatography. OsMaT-2 utilized a variety of flavonoid glucosides, including flavanone glucosides, flavone glucosides, flavonol glucosides, and isoflavone glucosides as substrates, but did not utilize anthocyanin. As an acyl donor, OsMaT-2 utilized only malonyl-CoA. Based on reactions with various quercetin 3-O-sugars, we identified the probable position of malonylation as the 6''-hydroxyl group of the sugar. This is the first report, to the best of our knowledge, of the cloning of a flavonoid malonyltransferase from O. sativa.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyltransferases / genetics
  • Acyltransferases / metabolism
  • Carbohydrates
  • Chromatography, Affinity
  • Cloning, Molecular
  • DNA, Complementary
  • DNA, Plant
  • Malonyl Coenzyme A
  • Oryza / enzymology*
  • Oryza / genetics
  • Phylogeny
  • Plant Proteins / genetics*
  • Plant Proteins / metabolism
  • Plants, Genetically Modified
  • Quercetin
  • RNA, Plant / isolation & purification
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Substrate Specificity


  • Carbohydrates
  • DNA, Complementary
  • DNA, Plant
  • Plant Proteins
  • RNA, Plant
  • Recombinant Proteins
  • Malonyl Coenzyme A
  • Quercetin
  • Acyltransferases