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- W2094324185 abstract "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." @default.
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- W2094324185 date "2010-04-01" @default.
- W2094324185 modified "2023-10-13" @default.
- W2094324185 title "An arginyl residue in rice UDP-arabinopyranose mutase is required for catalytic activity and autoglycosylation" @default.
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- W2094324185 doi "https://doi.org/10.1016/j.carres.2010.01.008" @default.
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