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  • Title: Identification and characterization of the BAHD acyltransferase malonyl CoA: anthocyanidin 5-O-glucoside-6''-O-malonyltransferase (At5MAT) in Arabidopsis thaliana.
    Author: D'Auria JC, Reichelt M, Luck K, Svatos A, Gershenzon J.
    Journal: FEBS Lett; 2007 Mar 06; 581(5):872-8. PubMed ID: 17292360.
    Abstract:
    The major anthocyanin in A. thaliana is a cyanidin derivative modified by glycosylation as well as by the addition of three acyl moieties: malonyl, p-coumaroyl, and sinapoyl. We have isolated a member of the BAHD acyltransferase family which catalyzes this malonylation reaction by combining a reverse genetics approach with biochemical genomics. A mutant line containing a T-DNA insertion in At3g29590, the gene encoding the malonylating enzyme, is incapable of producing malonylated anthocyanins. Transgenic plants harboring an RNAi silencing cassette for At3g29590 demonstrate a positive correlation between reduction in the At3g29590 gene transcript and the decrease of malonylated anthocyanins. Transcript levels for both At3g29590 and the epistatic gene At4g14090, encoding 5-O-anthocyanin glucosyltransferase, increase in several plant lines as they accumulate anthocyanin pigments. Investigation of the heterologously expressed and purified malonylating enzyme showed that the activity is specific for malonyl-CoA and for anthocyanins with 5-O-glucosylation. The malonyl transfer itself occurs only to the 5-O-glucoside function, and not to any of the other sugar moieties present in A. thaliana anthocyanins. Hence, both in vivo and in vitro results define the activity of the At3g29590-encoded enzyme as an anthocyanin 5-O-glucoside-6''-O-malonyltransferase (At5MAT).
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