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Papers In Press, published online ahead of print October 27, 2004
J. Biol. Chem, 10.1074/jbc.M410537200
Submitted on September 13, 2004
Revised on October 21, 2004
Accepted on October 27, 2004

UDP-glucuronic acid: Anthocyanin glucuronosyltransferase from red daisy (Bellis perennis) flowers enzymology and phylogenetics of a novel glucuronosyltransferase involved in flower pigment biosynthesis

Shin'ya Sawada, Hirokazu Suzuki, Fumiko Ichimaida, Masa-atsu Yamaguchi, Takashi Iwashita, Yuko Fukui, Hisashi Hemmi, Tokuzo Nishino, and Toru Nakayama

Department of Biomolecular Engineering, Tohoku University, Sendai, Miyagi 980-8579

Corresponding Author: nakayama{at}seika.che.tohoku.ac.jp

In contrast to the wealth of biochemical and genetic information on vertebrate glucuronosyltransferases (UGATs), only limited information is available on the role and phylogenetics of plant UGATs. Here, we report on the purification, characterization, and cDNA cloning of a novel UGAT involved in the biosynthesis of flower pigments in the red daisy (Bellis perennis). The purified enzyme, BpUGAT, was a soluble monomeric enzyme with a molecular mass of 54 kDa and catalyzed the regiospecific transfer of a glucuronosyl unit from UDP-glucuronate to the 2-hydroxyl group of the 3-glucosyl moiety of cyanidin 3-O-6-O-malonylglucoside (Cy3MG), with a kcat value of 34 sec-1 at pH 7.0 and 30C. BpUGAT was highly specific for cyanidin 3-O-glucosides (e.g., Km for Cy3MG, 19 mu M) and UDP-glucuronate (Km, 476 mu M). The BpUGAT cDNA was isolated on the basis of the amino acid sequence of the purified enzyme. Quantitative PCR analysis showed that transcripts of BpUGAT could be specifically detected in red petals, consistent with the temporal and spatial distributions of enzyme activity in the plant, and also consistent with enzymes role in pigment biosynthesis. A sequence analysis revealed that BpUGAT is related to the GT1 family of the glycosyltransferase superfamily (according to the CAZy database). Among GT1-family members that encompass vertebrate UGATs and plant secondary-product glycosyltransferases, the highest sequence similarity was found with flavonoid rhamnosyltransferases of plants (28~40% identity). Although the biological role (pigment biosynthesis) and enzymatic properties of BpUGAT are significantly different from those of vertebrate UGATs, both of these UGATs share a similarity, in that the product produced by these enzymes are more water-soluble, thus facilitating their accumulation in vacuoles (in BpUGAT) or their excretion from cells (in vertebrate UGATs), corroborating the proposed general significance of GT1-family members in the metabolism of small lipophilic molecules.


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