Journal
CARBOHYDRATE RESEARCH
Volume 345, Issue 6, Pages 787-791Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.carres.2010.01.008
Keywords
Arabinofuranose; Arginyl residue; Reversibly glycosylated polypeptides; Site-directed mutagenesis; UDP-arabinopyranose mutase
Funding
- Ministry of Agriculture, Forestry, and Fisheries of Japan [GMA-0007]
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Plants use UDP-arabinofuranose (UDP-Araf) to donate Araf residues in the biosynthesis of Araf-containing complex carbohydrates. UDP-Araf itself is formed from UDP-arabinopyranose (UDP-Arap) by UDP-arabinopyranose mutase (UAM). However, the mechanism by which this enzyme catalyzes the interconversion of UDP-Arap and UDP-Araf has not been determined. To gain insight into this reaction, functionally recombinant rUAMs were reacted with UDP-Glc or UDP-Araf. The glycosylated recombinant UAMs were fragmented with trypsin, and the glycopeptides formed were then identified and sequenced by LC-MS/MS. The results of these experiments, together with site-directed mutagenesis studies, suggest that in functional UAMs an arginyl residue is reversibly glycosylated with a single glycosyl residue, and that this residue is required for mutase activity. We also provide evidence that a DXD motif is required for catalytic activity. (C) 2010 Elsevier Ltd. All rights reserved.
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