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Plant and Cell Physiology Advance Access published online on June 27, 2009
Plant and Cell Physiology, doi:10.1093/pcp/pcp088
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© The Author 2009. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Functional and structural characterization of a flavonoid glucoside 1,6-glucosyltransferase from Catharanthus Roseus

Sayaka Masada1, Kazuyoshi Terasaka1, Yukie Oguchi1, Seiji Okazaki2,3, Tunehiro Mizushima1 and Hajime Mizukami1,*

1Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan
2Venture Business Laboratory, Nagoya University, Nagoya 464-8603, Japan

Corresponding Author: Prof. Hajime Mizukami, Graduate School of Pharmaceutical Sciences, Nagoya City University, Tanabe-dori 3-1, Mizuho-ku, Nagoya 467-8603, Japan, (Tel/Fax) +81-52-836-3415, (E-mail) hajimem{at}phar.nagoya-cu.ac.jp


  Abstract

Sugar-sugar glycosyltransferases play an important role in structural diversity of small molecule glycosides in higher plants. We isolated a cDNA clone encoding a sugar-sugar glucosyltransferase (CaUGT3) catalyzing 1,6-glucosylation of flavonol- and flavone glucosides for the first time from Catharanthus roseus. CaUGT3 exhibited a unique glucosyl chain elongation activity forming not only gentiobioside but also gentiotrioside and gentiotetroside in a sequential manner. We investigated the functional properties of CaUGT3 using homology modeling and site-directed mutagenesis, and identified amino acids positioned in the acceptor binding pocket as crucial for providing enough space to accommodate flavonoid glucosides instead of flavonoid aglycones. These results provide basic information for understanding and engineering the catalytic functions of sugar-sugar glycosyltransferases involved in biosynthesis of plant glycosides.

Keywords: Catharanthus roseus - Sugar-sugar glycosyltransferase - Flavonoid glucoside 1,6-Glucosyltransferase - Functional characterization - Homology modeling

3 Present address: Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki 305-0801, Japan

(Received April 11, 2009; Accepted June 16, 2009)
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