Purification and characterization of β-xylosidase that is active for plant complex type N-glycans from tomato (Solanum lycopersicum): removal of core α1-3 mannosyl residue is prerequisite for hy

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• 作者：Daisuke Yokouchi (1)
  Natsuko Ono (1)
  Kosuke Nakamura (2)
  Megumi Maeda (1) (3)
  Yoshinobu Kimura (1) (3)
  
• 关键词：β ; xylosidase ; Plant N ; glycan ; Fruit ripening ; Solanum lycopersicum
• 刊名：Glycoconjugate Journal
• 出版年：2013
• 出版时间：July 2013
• 年：2013
• 卷：30
• 期：5
• 页码：463-472
• 全文大小：647KB
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• 作者单位：Daisuke Yokouchi (1)
  Natsuko Ono (1)
  Kosuke Nakamura (2)
  Megumi Maeda (1) (3)
  Yoshinobu Kimura (1) (3)
  
  1. Department of Biofunctional Chemistry, Graduate School of Natural Science and Technology, Okayama University, Tsushima-Naka 1-1-1, Okayama, 700-8530, Japan
  2. Kagome Research Institute, Kagome Co., Ltd., 17 Nishitomiyama, Nasushiobara, Tochigi, 329-2762, Japan
  3. Department of Biofunctional Chemistry, Graduate School of Environmental and Life Science, Okayama University, Tsushima-Naka 1-1-1, Okayama, 700-8530, Japan
  
• ISSN：1573-4986

文摘

In this study, we purified and characterized the β-xylosidase involved in the turnover of plant complex type N-glycans to homogeneity from mature red tomatoes. Purified β-xylosidase (β-Xyl’ase Le-1) gave a single band with molecular masses of 67?kDa on SDS-PAGE under a reducing condition and 60?kDa on gelfiltration, indicating that β-Xyl’ase Le-1 has a monomeric structure in plant cells. The N-terminal amino acid could not be identified owing to a chemical modification. When pyridylaminated (PA-) N-glycans were used as substrates, β-Xyl’ase Le-1 showed optimum activity at about pH 5 at 40?°C, suggesting that the enzyme functions in a rather acidic circumstance such as in the vacuole or cell wall. β-Xyl’ase Le-1 hydrolyzed the β1-2 xylosyl residue from Man1Xyl1GlcNAc2-PA, Man1Xyl1Fuc1GlcNAc2-PA, and Man2Xyl1Fuc1GlcNAc2-PA, but not that from Man3Xyl1GlcNAc2-PA or Man3Xyl1Fuc1GlcNAc2-PA, indicating that the α1-3 arm mannosyl residue exerts significant steric hindrance for the access of β-Xyl’ase Le-1 to the xylosyl residue, whereas the α1-3 fucosyl residue exerts little effect. These results suggest that the release of the β1-2 xylosyl residue by β-Xyl’ase Le-1 occurs at least after the removal the α-1,3-mannosyl residue in the core trimannosyl unit.