4-硝基苯基-alpha-D-麦芽庚糖苷 | 74173-31-2

• 分子结构分类: 有机化合物 - 有机氧化合物
• 中文名称: 4-硝基苯基-alpha-D-麦芽庚糖苷
• 中文别名: (4-硝基苯基)-Α-D-麦芽七糖苷；(4-硝基苯基)-α-D-麦芽七糖苷
• 英文名称: p-nitrophenyl α-maltoheptaoside
• 英文别名: p-nitrophenylmaltoheptaoside；4-nitrophenyl O-α-d-glucopyranosyl-(1->4)-O-α-d-glucopyranosyl-(1->4)-O-α-d-glucopyranosyl-(1->4)-O-α-d-glucopyranosyl-(1->4)-O-α-d-glucopyranosyl-(1->4)-O-α-d-glucopyranosyl-(1->4)-α-d-glucopyranoside；4-Nitrophenyl maltoheptaoside；(2R,3R,4S,5S,6R)-2-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-4,5-dihydroxy-2-(hydroxymethyl)-6-(4-nitrophenoxy)oxan-3-yl]oxy-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol
• CAS: 74173-31-2
• 化学式: C₄₈H₇₅NO₃₈
• 分子量: 1274.11
• InChiKey: FSRMLWKBCQFLJA-HTZQGQHSSA-N

物化性质

• 沸点：
  1498.2±65.0 °C(Predicted)
• 密度：
  1.85±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -13.3
• 重原子数：
  87
• 可旋转键数：
  21
• 环数：
  8.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  620
• 氢给体数：
  22
• 氢受体数：
  38

反应信息

• 作为反应物：
  描述：

  4-硝基苯基-alpha-D-麦芽庚糖苷 、 二甲氧基乙烷 生成 4-Nitrophenyl 4,6-ethylidene-a-D-maltoheptaoside
  参考文献：
  名称：

  RAUSCHER, E.;SCHAICH, E.;NEUMANN, U.;WAHLEFELD, A.;GRUBER, W.;EMPL, B.

  摘要：

  DOI：
• 作为产物：
  描述：

  D-maltohexaose 、 对硝基苯-α-D-葡萄糖吡喃苷 以 甲醇 、 水 为溶剂， 反应 6.0h， 以13%的产率得到4-硝基苯基-alpha-D-麦芽庚糖苷
  参考文献：
  名称：

  Enzymatic Synthesis ofp-Nitrophenyl α-Maltoheptaoside by Transglycosylation of Maltohexaose-forming Amylase

  摘要：

  肺炎克雷伯氏菌突变体的细胞外麦芽六糖形成淀粉酶[EC 3.2.1.98]是一种正常的水解酶，可水解短链直链淀粉，得到约 40% 的麦芽六糖。通过在甲醇水溶液中使用麦芽六糖形成淀粉酶，可有效诱导从麦芽七糖到对硝基苯α-葡萄糖苷的 4 位的转糖基化。该酶以麦芽七糖为供体，对硝基苯基 α-葡萄糖苷为受体，特异性地生成了对硝基苯基 α-麦芽七糖苷（占对硝基苯基 α-葡萄糖苷的 13%）。对硝基苯α-麦芽庚糖苷的产量取决于甲醇溶剂的浓度、pH 值和温度。此外，在反应中使用甲醇水溶液体系不仅提高了对硝基苯α-葡萄糖苷的溶解度，还大大增加了对硝基苯α-马尔托庚苷的生成量，而马尔托庚苷是检测血清和尿液中人类淀粉酶的有效底物。

  DOI：

  10.1080/00021369.1990.10869998

文献信息

• The action of germinated barley alpha-amylases on linear maltodextrins
  作者：Alex.W. MacGregor、Joan E. Morgan、E.Ann MacGregor

  DOI：10.1016/0008-6215(92)85080-j

  日期：1992.4

  The actions of barley alpha-amylase isozymes 1 and 2 (EC 3.2.1.1) on malto-oligosaccharides and their p-nitrophenyl glycosides were similar, but not identical. For each isozyme, transglycosylation occurred with small substrates that were hydrolysed with difficulty, whereas the rates of hydrolysis increased with increase in the size of the substrate for both the malto-oligosaccharides and the p-nitrophenyl glycosides. A p-nitrophenyl group was found to mimic a glucose residue to a large extent. The differences in action of the isozymes are believed to be caused by differences at more than one subsite of the active site. A lysine-arginine substitution is postulated to account for some of the observed variations.
• RAUSCHER, E.;SCHAICH, E.;NEUMANN, U.;WAHLEFELD, A.;GRUBER, W.;EMPL, B.
  作者：RAUSCHER, E.、SCHAICH, E.、NEUMANN, U.、WAHLEFELD, A.、GRUBER, W.、EMPL, B.

  DOI：——

  日期：——
• Enzymatic Synthesis of<i>p</i>-Nitrophenyl α-Maltoheptaoside by Transglycosylation of Maltohexaose-forming Amylase
  作者：Koichi Ogawa、Osamu Uejima、Teruo Nakakuki、Taichi Usui、Keiji Kainuma

  DOI：10.1080/00021369.1990.10869998

  日期：1990.3

  An extracellular maltohexaose-forming amylase [EC 3.2.1.98] from Klebsiella pneumoniae mutant is a normal hydrolytic enzyme that hydrolyzes short-chain amylose to give about 40 % maltohexaose. Transglycosylation from maltoheptaose to the 4-position of p-nitrophenyl α-glucoside was efficiently induced through the use of maltohexaose-forming amylase in an aqueous methanol solution. The enzyme specifically produced p-nitrophenyl α-maltoheptaoside (13 % of the p-nitrophenyl α-glucoside) from maltoheptaose as a donor and p-nitrophenyl α-glucoside as an acceptor. The yield of p-nitrophenyl α-maltoheptaoside depended on the concentration of methanol solvent, the pH, and temperature. Furthermore, the use of the aqueous methanol system in the reaction not only improved the solubility of p-nitrophenyl α-glucoside but also greatly increased the formation of p-nitrophenyl α-maltoheptaoside, which is a useful substrate for assay of human amylase in serum and urine.

  肺炎克雷伯氏菌突变体的细胞外麦芽六糖形成淀粉酶[EC 3.2.1.98]是一种正常的水解酶，可水解短链直链淀粉，得到约 40% 的麦芽六糖。通过在甲醇水溶液中使用麦芽六糖形成淀粉酶，可有效诱导从麦芽七糖到对硝基苯α-葡萄糖苷的 4 位的转糖基化。该酶以麦芽七糖为供体，对硝基苯基 α-葡萄糖苷为受体，特异性地生成了对硝基苯基 α-麦芽七糖苷（占对硝基苯基 α-葡萄糖苷的 13%）。对硝基苯α-麦芽庚糖苷的产量取决于甲醇溶剂的浓度、pH 值和温度。此外，在反应中使用甲醇水溶液体系不仅提高了对硝基苯α-葡萄糖苷的溶解度，还大大增加了对硝基苯α-马尔托庚苷的生成量，而马尔托庚苷是检测血清和尿液中人类淀粉酶的有效底物。