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Title: Molecular characteristics of plant UDP-arabinopyranose mutases

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.

Authors:
 [1];  [2];  [1]; ORCiD logo [1]
  1. Technical Univ. of Denmark, Roskilde (Denmark)
  2. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); Univ. of California, Berkeley, CA (United States)
Publication Date:
Research Org.:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
OSTI Identifier:
1573880
Alternate Identifier(s):
OSTI ID: 1560694; OSTI ID: 1576508
Grant/Contract Number:  
AC02-05CH11231
Resource Type:
Published Article
Journal Name:
Glycobiology
Additional Journal Information:
Journal Volume: 29; Journal Issue: 12; Journal ID: ISSN 1460-2423
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Saqib, Anam, Scheller, Henrik Vibe, Fredslund, Folmer, and Welner, Ditte Hededam. Molecular characteristics of plant UDP-arabinopyranose mutases. United States: N. p., 2019. Web. doi:10.1093/glycob/cwz067.
Saqib, Anam, Scheller, Henrik Vibe, Fredslund, Folmer, & Welner, Ditte Hededam. Molecular characteristics of plant UDP-arabinopyranose mutases. United States. doi:10.1093/glycob/cwz067.
Saqib, Anam, Scheller, Henrik Vibe, Fredslund, Folmer, and Welner, Ditte Hededam. Wed . "Molecular characteristics of plant UDP-arabinopyranose mutases". United States. doi:10.1093/glycob/cwz067.
@article{osti_1573880,
title = {Molecular characteristics of plant UDP-arabinopyranose mutases},
author = {Saqib, Anam and Scheller, Henrik Vibe and Fredslund, Folmer and Welner, Ditte Hededam},
abstractNote = {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.},
doi = {10.1093/glycob/cwz067},
journal = {Glycobiology},
number = 12,
volume = 29,
place = {United States},
year = {2019},
month = {5}
}

Journal Article:
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DOI: 10.1093/glycob/cwz067

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