6-O(β-D-Glucopyranosyluronsaeure)-D-galactose | 1693-80-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 6-O(β-D-Glucopyranosyluronsaeure)-D-galactose
• 英文别名: GlcA(b1-6)Gal；(2S,3S,4S,5R,6R)-3,4,5-trihydroxy-6-[[(2R,3R,4S,5R)-3,4,5,6-tetrahydroxyoxan-2-yl]methoxy]oxane-2-carboxylic acid
• CAS: 1693-80-7
• 化学式: C₁₂H₂₀O₁₂
• 分子量: 356.284
• InChiKey: YOOPHLDCWPOWDX-VTTLBJKKSA-N

物化性质

• 沸点：
  723.3±60.0 °C(Predicted)
• 密度：
  1.86±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -4.5
• 重原子数：
  24
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.92
• 拓扑面积：
  207
• 氢给体数：
  8
• 氢受体数：
  12

反应信息

• 作为反应物：
  描述：

  6-O(β-D-Glucopyranosyluronsaeure)-D-galactose 在 serNcGlc*of*Neurospora*crassa*OR₇₄A 作用下， 以 acetate buffer 为溶剂， 生成 D-吡喃葡萄糖醛酸
  参考文献：
  名称：

  Properties of family 79 β-glucuronidases that hydrolyze β-glucuronosyl and 4-O-methyl-β-glucuronosyl residues of arabinogalactan-protein

  摘要：

  The carbohydrate moieties of arabinogalactan-proteins (AGPs), which are mainly composed of Gal, L-Ara, GlcA, and 4Me-GlcA residues, are essential for the physiological functions of these proteoglycans in higher plants. For this study, we have identified two genes encoding family 79 beta-glueuronidases, designated AnGlcAase and NcGlcAase, in Aspergillus niger and Neurospora crassa, respectively, based on the amino acid sequence of a native beta-glucuronidase purified from a commercial pectolytic enzyme preparation from A. niger. Although the deduced protein sequences of AnGlcAase and NcGlcAase were highly similar, the recombinant enzymes expressed in Pichia pastoris exhibited distinct substrate specificity toward 4-Me-GlcA residues of AGPs: recombinant ADGlcAase (rAnGlcAase) substantially liberated both GlcA and 4-Me-GlcA residues from radish AGPs, whereas recombinant NcGlcAase (rNcGlcAase) activity on the 4-Me-GlcA residues of AGPs was very low. Maximum activity of rAnGlcAase hydrolyzing PNP beta-GlcA occurred at pH 3.0-4.0, whereas the maximum rNcGlcAase activity was at pH 6.0. The apparent K. values of rAnGlcAase were 30.4 mu M for PNP beta-GlcA and 422 mu M for beta-GIcA-(1 -> 6)-Gal, and those of rNcGlcAase were 38.3 mu M and 378 mu M, respectively. Similar to the native enzyme, rAnGlcAase was able to catalyze the transglycosylation of GlcA residues from PNP beta-GlcA to various monosaccharide acceptors such as Glc, Gal, and Xyl. We propose that both AnGlcAase and NcGlcAase are instances of a novel type of beta-glucuronidase with the capacity to hydrolyze beta-GlcA and 4-Me-beta-GlcA residues of AGPs, although they differ significantly in their preferences. (c) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2008.03.004

文献信息

• Properties of family 79 β-glucuronidases that hydrolyze β-glucuronosyl and 4-O-methyl-β-glucuronosyl residues of arabinogalactan-protein
  作者：Tomoyuki Konishi、Toshihisa Kotake、Dina Soraya、Koji Matsuoka、Tetsuo Koyama、Satoshi Kaneko、Kiyohiko Igarashi、Masahiro Samejima、Yoichi Tsumuraya

  DOI：10.1016/j.carres.2008.03.004

  日期：2008.5

  The carbohydrate moieties of arabinogalactan-proteins (AGPs), which are mainly composed of Gal, L-Ara, GlcA, and 4Me-GlcA residues, are essential for the physiological functions of these proteoglycans in higher plants. For this study, we have identified two genes encoding family 79 beta-glueuronidases, designated AnGlcAase and NcGlcAase, in Aspergillus niger and Neurospora crassa, respectively, based on the amino acid sequence of a native beta-glucuronidase purified from a commercial pectolytic enzyme preparation from A. niger. Although the deduced protein sequences of AnGlcAase and NcGlcAase were highly similar, the recombinant enzymes expressed in Pichia pastoris exhibited distinct substrate specificity toward 4-Me-GlcA residues of AGPs: recombinant ADGlcAase (rAnGlcAase) substantially liberated both GlcA and 4-Me-GlcA residues from radish AGPs, whereas recombinant NcGlcAase (rNcGlcAase) activity on the 4-Me-GlcA residues of AGPs was very low. Maximum activity of rAnGlcAase hydrolyzing PNP beta-GlcA occurred at pH 3.0-4.0, whereas the maximum rNcGlcAase activity was at pH 6.0. The apparent K. values of rAnGlcAase were 30.4 mu M for PNP beta-GlcA and 422 mu M for beta-GIcA-(1 -> 6)-Gal, and those of rNcGlcAase were 38.3 mu M and 378 mu M, respectively. Similar to the native enzyme, rAnGlcAase was able to catalyze the transglycosylation of GlcA residues from PNP beta-GlcA to various monosaccharide acceptors such as Glc, Gal, and Xyl. We propose that both AnGlcAase and NcGlcAase are instances of a novel type of beta-glucuronidase with the capacity to hydrolyze beta-GlcA and 4-Me-beta-GlcA residues of AGPs, although they differ significantly in their preferences. (c) 2008 Elsevier Ltd. All rights reserved.