Journal
GLYCOBIOLOGY
Volume 29, Issue 12, Pages 839-846Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwz067
Keywords
arabinofuranose; arabinose; reversibly glycosylated polypeptide; UDP-arabinopyranose mutase; UDP-arabinose
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Funding
- Novo Nordisk Foundation [NNF10CC1016517]
- US Department of Energy, Office of Science, Office of Biological and Environmental Research [DE-AC02-05CH11231]
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L-Arabinofuranose is a ubiquitous component of the cell wall and various natural products in plants, where it is synthesized from cytosolic UDP-arabinopyranose (UDP-Arap). The biosynthetic machinery long remained enigmatic in terms of responsible enzymes and subcellular localization. With the discovery of UDP-Arap mutase in plant cytosol, the demonstration of its role in cell-wall arabinose incorporation and the identification of UDP-arabinofuranose transporters in the Golgi membrane, it is clear that the cytosolic UDP-Arap mutases are the key enzymes converting UDP-Arap to UDP-arabinofuranose for cell wall and natural product biosynthesis. This has recently been confirmed by several genotype/phenotype studies. In contrast to the solid evidence pertaining to UDP-Arap mutase function in vivo, the molecular features, including enzymatic mechanism and oligomeric state, remain unknown. However, these enzymes belong to the small family of proteins originally identified as reversibly glycosylated polypeptides (RGPs), which has been studied for >20 years. Here, we review the UDP-Arap mutase and RGP literature together, to summarize and systemize reported molecular characteristics and relations to other proteins.
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