@article {Berger:2006p7995,
	title = {Rosmarinic acid synthase is a new member of the superfamily of BAHD acyltransferases},
	journal = {Planta},
	volume = {224},
	number = {6},
	year = {2006},
	month = {Nov},
	pages = {1503{\textendash}10},
	abstract = {Purification of rosmarinic acid synthase (hydroxycinnamoyl-CoA:hydroxyphenyllactate 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 PCR-based approach to isolate the full-length 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 47,932 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 4-coumaroyl- and caffeoyl-coenzyme A and 4-hydroxyphenyllactate as well as 3.4-dihydroxyphenyllactate as substrates. Shikimic acid and quinic acid were not able to serve as hydroxycinnamoyl acceptors. This therefore is the first report of the cDNA-cloning of a rosmarinic acid synthase.},
	keywords = {Acyltransferases, Amino Acid Sequence, Base Sequence, DNA: Complementary, Molecular Sequence Data, Phylogeny, Polymerase Chain Reaction},
	doi = {10.1007/s00425-006-0393-y},
	author = {Anja Berger and Juliane Meinhard and Maike Petersen}
}
@article {Hirotani:2000p8040,
	title = {Cloning and expression of UDP-glucose: flavonoid 7-O-glucosyltransferase from hairy root cultures of Scutellaria baicalensis},
	journal = {Planta},
	volume = {210},
	number = {6},
	year = {2000},
	month = {May},
	pages = {1006{\textendash}13},
	abstract = {A cDNA encoding UDP-glucose: baicalein 7-O-glucosyltransferase (UBGT) was isolated from a cDNA library from hairy root cultures of Scutellaria baicalensis Georgi probed with a partial-length cDNA clone of a UDP-glucose: flavonoid 3-O-glucosyltransferase (UFGT) from grape (Vitis vinifera L.). The heterologous probe contained a glucosyltransferase consensus amino acid sequence which was also present in the Scutellaria cDNA clones. The complete nucleotide sequence of the 1688-bp cDNA insert was determined and the deduced amino acid sequences are presented. The nucleotide sequence analysis of UBGT revealed an open reading frame encoding a polypeptide of 476 amino acids with a calculated molecular mass of 53,094 Da. The reaction product for baicalein and UDP-glucose catalyzed by recombinant UBGT in Escherichia coli was identified as authentic baicalein 7-O-glucoside using high-performance liquid chromatography and proton nuclear magnetic resonance spectroscopy. The enzyme activities of recombinant UBGT expressed in E. coli were also detected towards flavonoids such as baicalein, wogonin, apigenin, scutellarein, 7,4{\textquoteright}-dihydroxyflavone and kaempferol, and phenolic compounds. The accumulation of UBGT mRNA in hairy roots was in response to wounding or salicylic acid treatments.},
	keywords = {Amino Acid Sequence, Blotting: Northern, Chromatography: High Pressure Liquid, Cloning: Molecular, Escherichia coli, Flavonoids, Glucosyltransferases, Lamiaceae, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Phylogeny, Plant Roots, Recombinant Proteins},
	author = {M Hirotani and R Kuroda and H Suzuki and T Yoshikawa}
}
