Plant Physiology and Biochemistry 2009-01-01

Molecular characterization of flavonoid malonyltransferase from Oryza sativa.

Dea Hwan Kim, Seong Kyong Kim, Jeong-Ho Kim, Bong-Gyu Kim, Joong-Hoon Ahn

Index: Plant Physiol. Biochem. 47 , 991-997, (2009)

Full Text: HTML

Abstract

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.

Related Compounds

Structure Name/CAS No. Articles
Malonyl coenzyme A tetralithium salt Structure Malonyl coenzyme A tetralithium salt
CAS:116928-84-8