β-GlcpA-(1->3)-Galp | 4343-50-4

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: β-GlcpA-(1->3)-Galp
• 英文别名: β-GlcA-(1->3)-Gal；3-O-(β-D-Glucopyranosyluronsaeure)-D-galactose；GlcA(b1-3)Gal；(2S,3S,4S,5R,6R)-3,4,5-trihydroxy-6-[(3R,4S,5S,6R)-2,3,5-trihydroxy-6-(hydroxymethyl)oxan-4-yl]oxyoxane-2-carboxylic acid
• CAS: 4343-50-4
• 化学式: C₁₂H₂₀O₁₂
• 分子量: 356.284
• InChiKey: GGFHJVYVXSKMOX-HUOUOSQISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.9
• 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

• 作为产物：
  描述：

  D-吡喃葡萄糖 、 6-O(β-D-Glucopyranosyluronsaeure)-D-galactose 、 4-硝基苯-Β-D-葡萄糖苷酸 在 serAnGlc*of*Aspergillus*niger*van*Tieghem*(ATCC*22343) 作用下， 以 acetate buffer 为溶剂， 生成 β-GlcpA-(1->3)-Galp
  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

• The capsular polysaccharide of klebsiella serotype K60; a novel, structural pattern
  作者：Guy G.S. Dutton、Jose Di Fabio

  DOI：10.1016/s0008-6215(00)85197-6

  日期：1980.12

  Non-linear capsular polysaccharides of Klebsiella bacteria usually have a single side-chain per repeating unit, or, less commonly, two side-chains attached to the same unit. The capsular polysaccharide from Klebsiella serotype K60 is unique in having three side-chains in the heptasaccharide repeating-unit shown. The structure, including the configuration of the glycosidic linkages, was established

  克雷伯氏菌细菌的非线性荚膜多糖通常每个重复单元有一条侧链，或者较不常见的是，两条重复链附着在同一单元上。来自克雷伯氏菌血清型K60的荚膜多糖的独特之处在于在所示的七糖重复单元中具有三个侧链。包括糖苷键构型在内的结构主要是通过表征寡糖来确定的，该寡糖是通过原始水解，荚膜多糖和聚合物的部分水解而得到的，该水解是通过侧链的Smith降解去除的（式，参见文本）。
• 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.