کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1388538 | 982801 | 2010 | 5 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: An arginyl residue in rice UDP-arabinopyranose mutase is required for catalytic activity and autoglycosylation An arginyl residue in rice UDP-arabinopyranose mutase is required for catalytic activity and autoglycosylation](/preview/png/1388538.png)
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.
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Journal: Carbohydrate Research - Volume 345, Issue 6, 19 April 2010, Pages 787–791