甘露四糖 | 51327-76-5

• 分子结构分类: 有机化合物 - 有机氧化合物
• 中文名称: 甘露四糖
• 英文名称: mannotetraose
• 英文别名: (2S,3R,4R,5R)-4-(((2S,3S,4R,5S,6R)-5-(((2S,3S,4R,5S,6R)-3,4-Dihydroxy-6-(hydroxymethyl)-5-(((2S,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl)oxy)tetrahydro-2H-pyran-2-yl)oxy)-3,4-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl)oxy)-2,3,5,6-tetrahydroxyhexanal；(2S,3R,4R,5R)-4-[(2S,3S,4R,5S,6R)-5-[(2S,3S,4R,5S,6R)-3,4-dihydroxy-6-(hydroxymethyl)-5-[(2S,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-2,3,5,6-tetrahydroxyhexanal
• CAS: 51327-76-5
• 化学式: C₂₄H₄₂O₂₁
• 分子量: 666.585
• InChiKey: UYQJCPNSAVWAFU-UIQXVFQFSA-N

物化性质

• 熔点：
  231.5-232.0 °C
• 沸点：
  1116.9±65.0 °C(Predicted)
• 密度：
  1.79±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -9.3
• 重原子数：
  45
• 可旋转键数：
  14
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.96
• 拓扑面积：
  356
• 氢给体数：
  14
• 氢受体数：
  21

反应信息

• 作为反应物：
  描述：

  甘露四糖 在 recombinant glycoside hydrolase family 26 mannanase from the symbiotic protist of the lower termite Reticulitermes speratus 作用下， 以 aq. buffer 为溶剂， 反应 1.0h， 生成 4-O-（bD-甘露吡喃糖基）-D-甘露糖
  参考文献：
  名称：

  The GH26 β-mannanase RsMan26H from a symbiotic protist of the termite Reticulitermes speratus is an endo-processive mannobiohydrolase: Heterologous expression and characterization

  摘要：

  Symbiotic protists in the gut of termites are prominent natural resources for enzymes involved in lignocellulose degradation. Here we report expression, purification, and biochemical characterization of a glycoside hydrolase family 26 mannanase RsMan26H from the symbiotic protist of the lower termite, Reticulitermes speratus. Biochemical analysis of RsMan26H demonstrates that this enzyme is an endo-processive mannobiohydrolase producing mannobiose from oligo- and polysaccharides, followed by a minor accumulation of oligosaccharides larger than mannobiose. To our knowledge, this is the first report describing the unique mannobiohydrolase enzyme from the eukaryotic origin. (C) 2014 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.bbrc.2014.08.103
• 作为产物：
  描述：

  alkaline earth salt of/the/ methylsulfuric acid 在 硫酸 、 乙酸酐 、 溶剂黄146 作用下， 生成 甘露四糖
  参考文献：
  名称：

  Aspinall et al., Journal of the Chemical Society, 1958, p. 215,218, 220

  摘要：

  DOI：

文献信息

• Enzymatic synthesis and polymerisation of β-mannosyl acrylates produced from renewable hemicellulosic glycans
  作者：Anna Rosengren、Samuel J. Butler、Monica Arcos-Hernandez、Karl-Erik Bergquist、Patric Jannasch、Henrik Stålbrand

  DOI：10.1039/c8gc03947j

  日期：——

  We show that glycoside hydrolases can catalyse the synthesis of glycosyl acrylate monomers using renewable hemicellulose as a glycosyl donor, and we also demonstrate the preparation of novel glycopolymers by radical polymerisation of these monomers. For this, two family 5 β-mannanases (TrMan5A from Trichoderma reesei and AnMan5B from Aspergillus niger) were evaluated for their transglycosylation capacity

  我们表明，糖苷水解酶可以使用可再生半纤维素作为糖基供体，催化丙烯酸糖基丙烯酸酯单体的合成，并且我们还证明了通过这些单体的自由基聚合制备新型糖聚合物。为此，使用了两个家族5β-甘露聚糖酶（来自里氏木霉的Tr Man5A和来自黑曲霉的An Man5B使用甲基丙烯酸2-羟乙酯（HEMA）作为糖基受体评估它们的转糖基化能力。如使用MALDI-ToF质谱（MS）作为初始产物筛选方法所分析的，两种酶均催化甘露寡糖和HEMA之间的结合。两种酶在HEMA和烯丙醇作为受体分子的作用下具有不同的产物谱（糖基供体长度）。一个Man5A似乎更喜欢糖受体与所期望的烯丙基和HEMA缀合物检测到的峰强度降低MS。与An Man5A相比，Tr Man5A在HEMA-糖缀合物中显示出明显的MS峰。Tr已显示，Man5A使用刺槐豆胶半乳甘露聚糖或软木半纤维素（乙酰半乳葡甘露聚糖）作为供体底物，催化合成β-甘露糖基丙烯酸酯。使
• Novel β-1,4-Mannanase Belonging to a New Glycoside Hydrolase Family in Aspergillus nidulans
  作者：Motoyuki Shimizu、Yuhei Kaneko、Saaya Ishihara、Mai Mochizuki、Kiyota Sakai、Miyuki Yamada、Shunsuke Murata、Eriko Itoh、Tatsuya Yamamoto、Yu Sugimura、Tatsuya Hirano、Naoki Takaya、Tetsuo Kobayashi、Masashi Kato

  DOI：10.1074/jbc.m115.661645

  日期：2015.11

  Many filamentous fungi produce beta-mannan-degrading beta-1,4-mannanases that belong to the glycoside hydrolase 5 (GH5) and GH26 families. Here we identified a novel beta-1,4-mannanase (Man134A) that belongs to a new glycoside hydrolase (GH) family (GH134) in Aspergillus nidulans. Blast analysis of the amino acid sequence using the NCBI protein database revealed that this enzyme had no similarity to any sequences and no putative conserved domains. Protein homologs of the enzyme were distributed to limited fungal and bacterial species. Man134A released mannobiose (M-2), mannotriose (M-3), and mannotetraose (M-4) but not mannopentaose (M-5) or higher manno-oligosaccharides when galactose-free beta-mannan was the substrate from the initial stage of the reaction, suggesting that Man134A preferentially reacts with beta-mannan via a unique catalytic mode. Man134A had high catalytic efficiency (k(cat)/K-m) toward mannohexaose (M-6) compared with the endo-beta-1,4-mannanase Man5C and notably converted M-6 to M-2, M-3, and M-4, with M-3 being the predominant reaction product. The action of Man5C toward beta-mannans was synergistic. The growth phenotype of a Man134A disruptant was poor when beta-mannans were the sole carbon source, indicating that Man134A is involved in beta-mannan degradation in vivo. These findings indicate a hitherto undiscovered mechanism of beta-mannan degradation that is enhanced by the novel beta-1,4-mannanase, Man134A, when combined with other mannanolytic enzymes including various endo-beta-1,4-mannanases.
• The GH26 β-mannanase RsMan26H from a symbiotic protist of the termite Reticulitermes speratus is an endo-processive mannobiohydrolase: Heterologous expression and characterization
  作者：Hikaru Tsukagoshi、Akihiko Nakamura、Takuya Ishida、Masato Otagiri、Shigeharu Moriya、Masahiro Samejima、Kiyohiko Igarashi、Katsuhiko Kitamoto、Manabu Arioka

  DOI：10.1016/j.bbrc.2014.08.103

  日期：2014.9

  Symbiotic protists in the gut of termites are prominent natural resources for enzymes involved in lignocellulose degradation. Here we report expression, purification, and biochemical characterization of a glycoside hydrolase family 26 mannanase RsMan26H from the symbiotic protist of the lower termite, Reticulitermes speratus. Biochemical analysis of RsMan26H demonstrates that this enzyme is an endo-processive mannobiohydrolase producing mannobiose from oligo- and polysaccharides, followed by a minor accumulation of oligosaccharides larger than mannobiose. To our knowledge, this is the first report describing the unique mannobiohydrolase enzyme from the eukaryotic origin. (C) 2014 Elsevier Inc. All rights reserved.
• Aspinall et al., Journal of the Chemical Society, 1958, p. 215,218, 220
  作者：Aspinall et al.

  DOI：——

  日期：——