Molecular characteristics of plant UDP-arabinopyranose mutases

Anam Saqib, Henrik Vibe Scheller, Folmer Fredslund, Ditte Hededam Welner

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Abstract

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.
Original languageEnglish
JournalGlycobiology
Volume29
Issue number12
Pages (from-to)839-846
ISSN0959-6658
DOIs
Publication statusPublished - 2019

Keywords

  • Arabinofuranose
  • Arabinose
  • Reversibly glycosylated polypeptide
  • UDP-arabinopyranose mutase
  • UDP-arabinose

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