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Title of Journal: Planta

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Abbravation: Planta

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Springer-Verlag

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10.1002/syn.890010408

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1432-2048

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Rosmarinic acid synthase is a new member of the su

Authors: Anja Berger Juliane Meinhard Maike Petersen
Publish Date: 2006/09/19
Volume: 224, Issue: 6, Pages: 1503-1510
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Abstract

Purification of rosmarinic acid synthase hydroxycinnamoylCoAhydroxyphenyllactate hydroxycinnamoyltransferase from suspension cells of Coleus blumei Benth Lamiaceae by fractionated ammonium sulphate precipitation hydrophobic interaction chromatography and two affinity chromatography steps led to the identification of peptide sequences which enabled a PCRbased approach to isolate the fulllength cDNA encoding this enzyme The open reading frame of the cDNA had a length of 1290 base pairs encoding a protein of 430 amino acid residues with a molecular mass of 47932 Da with typical characteristics of an acyltransferase of the BAHD superfamily The cDNA was heterologously expressed in Escherichia coli The enzyme displayed the activity of rosmarinic acid synthase using 4coumaroyl and caffeoylcoenzyme A and 4hydroxyphenyllactate as well as 34dihydroxyphenyllactate as substrates Shikimic acid and quinic acid were not able to serve as hydroxycinnamoyl acceptors This therefore is the first report of the cDNAcloning of a rosmarinic acid synthase

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