mannohexaose

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: mannohexaose
• 英文别名: Man(b1-4)Man(b1-4)Man(b1-4)Man(b1-4)Man(b1-4)aldehydo-Man；(2S,3R,4R,5R)-4-[(2S,3S,4R,5S,6R)-5-[(2S,3S,4R,5S,6R)-5-[(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-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-2,3,5,6-tetrahydroxyhexanal
• 化学式: C₃₆H₆₂O₃₁
• 分子量: 990.87
• InChiKey: DJMVHSOAUQHPSN-BDEBKWNZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -13.6
• 重原子数：
  67
• 可旋转键数：
  20
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.97
• 拓扑面积：
  514
• 氢给体数：
  20
• 氢受体数：
  31

反应信息

• 作为反应物：
  描述：

  mannohexaose 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 2.0h， 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

文献信息

• 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.