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Plant Physiology Preview Published on March 21, 2008; 10.1104/pp.107.115576
Received December 26, 2007 UDP-xylose stimulated glucuronyltransferase activity in wheat (Triticum aestivum L.) microsomal membranes: Characterization and role in glucurono(arabino)xylan biosynthesis
Department of Environmental and Plant Biology, Molecular and Cellular Biology Program, Ohio University, Athens, OH 45701, USA * Corresponding author; email: faik{at}ohio.edu.
Microsomal membranes from etiolated wheat (Triticum aestivum L.) seedlings cooperatively incorporated xylose, arabinose, and glucuronic acid residues from their corresponding uridine 5'-diphosphosugars into an ethanol-insoluble glucurono(arabino)xylan(GAX)-like product. A glucuronyltransferase activity that is enhanced by the presence of uridine diphosphate xylose was also identified in these microsomes. Wheat glucuronyltransferase activity was optimal at pH7, required manganese ions, and several lines of evidence suggest its involvement in GAX-like biosynthesis. The GAX characteristics of the [14C]product were confirmed by digestion with a purified endo-xylanase from Aspergillus awamori (endo-xylanase III) and by total acid hydrolysis resulting in a xylose:arabinose:glucuronic acid molar ratio of
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