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Endo M, Kotake T, Watanabe Y, et al. Biosynthesis of the carbohydrate moieties of arabinogalactan proteins by membrane-bound β-glucuronosyltransferases from radish primary roots. Planta. 2013;238(6):1157-69doi: 10.1007/s00425-013-1959-0.
Endo, M., Kotake, T., Watanabe, Y., Kimura, K., & Tsumuraya, Y. (2013). Biosynthesis of the carbohydrate moieties of arabinogalactan proteins by membrane-bound β-glucuronosyltransferases from radish primary roots. Planta, 238(6), 1157-69. https://doi.org/10.1007/s00425-013-1959-0
Endo, Maya, et al. "Biosynthesis of the carbohydrate moieties of arabinogalactan proteins by membrane-bound β-glucuronosyltransferases from radish primary roots." Planta vol. 238,6 (2013): 1157-69. doi: https://doi.org/10.1007/s00425-013-1959-0
Endo M, Kotake T, Watanabe Y, Kimura K, Tsumuraya Y. Biosynthesis of the carbohydrate moieties of arabinogalactan proteins by membrane-bound β-glucuronosyltransferases from radish primary roots. Planta. 2013 Dec;238(6):1157-69. doi: 10.1007/s00425-013-1959-0. Epub 2013 Sep 22. PMID: 24057431; PMCID: PMC3898515.
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Planta. 2013 Dec;238(6):1157-69. doi: 10.1007/s00425-013-1959-0. Epub 2013 Sep 22.

Biosynthesis of the carbohydrate moieties of arabinogalactan proteins by membrane-bound β-glucuronosyltransferases from radish primary roots.

Planta

Maya Endo, Toshihisa Kotake, Yoko Watanabe, Kazumasa Kimura, Yoichi Tsumuraya

Affiliations

  1. Division of Life Science, Graduate School of Science and Engineering, Saitama University, 255 Shimo-okubo, Sakura-ku, Saitama, 338-8570, Japan.
  2. Yakult Central Institute for Microbiological Research, 1796 Yaho, Kunitachi, Tokyo, 186-8650, Japan.
  3. Division of Life Science, Graduate School of Science and Engineering, Saitama University, 255 Shimo-okubo, Sakura-ku, Saitama, 338-8570, Japan. [email protected].

PMID: 24057431 PMCID: PMC3898515 DOI: 10.1007/s00425-013-1959-0

Abstract

A membrane fraction from etiolated 6-day-old primary radish roots (Raphanus sativus L. var hortensis) contained β-glucuronosyltransferases (GlcATs) involved in the synthesis of the carbohydrate moieties of arabinogalactan proteins (AGPs). The GlcATs transferred [(14)C]GlcA from UDP-[(14)C]GlcA on to β-(1 → 3)-galactan as an exogenous acceptor substrate, giving a specific activity of 50-150 pmol min(-1) (mg protein)(-1). The enzyme specimen also catalyzed the transfer of [(14)C]GlcA on to an enzymatically modified AGP from mature radish root. Analysis of the transfer products revealed that the transfer of [(14)C]GlcA occurred preferentially on to consecutive (1 → 3)-linked β-Gal chains as well as single branched β-(1 → 6)-Gal residues through β-(1 → 6) linkages, producing branched acidic side chains. The enzymes also transferred [(14)C]GlcA residues on to several oligosaccharides, such as β-(1 → 6)- and β-(1 → 3)-galactotrioses. A trisaccharide, α-L-Araf-(1 → 3)-β-Gal-(1 → 6)-Gal, was a good acceptor, yielding a branched tetrasaccharide, α-L-Araf-(1 → 3)[β-GlcA-(1 → 6)]-β-Gal-(1 → 6)-Gal. We report the first in vitro assay system for β-GlcATs involved in the AG synthesis as a step toward full characterization and cloning.

Keywords: Cell wall; Glucuronic acid; Glycosyltransferase; Raphanus

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