maltoheptaose | 4202-44-2

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: maltoheptaose
• 英文别名: Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a1-4)a-Glc；(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-[(2R,3S,4R,5R,6S)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-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: 4202-44-2
• 化学式: C₄₈H₈₂O₄₁
• 分子量: 1315.15
• InChiKey: RUJILUJOOCOSRO-WJMYNTJYSA-N

物化性质

• 沸点：
  1540.0±65.0 °C(Predicted)
• 密度：
  1.89±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -17.6
• 重原子数：
  89
• 可旋转键数：
  22
• 环数：
  8.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  664
• 氢给体数：
  26
• 氢受体数：
  41

反应信息

• 作为反应物：
  描述：

  maltoheptaose 在 sodium dihydrogenphosphate 作用下， 以 水 为溶剂， 生成 maltoheptaose
  参考文献：
  名称：

  Determination of kinetic parameters for maltotriose and higher malto-oligosaccharides in the reactions catalyzed by α-d-glucan phosphorylase from potato

  摘要：

  For kinetic studies on its synthetic and phosphorolytic reactions, alpha-D-glucan phosphorylase form potatoes was purified chromatographically until free of D-enzyme. Purified maltotriose (G3) is a poor primer in the phosphorylase-catalyzed synthetic reaction, showing an anomalous time course and making previous attempts to determine its kinetic parameters unsuccessful. In the present work the true rate of the G3-primed reaction was obtained from linear plots obtained by incorporating a sufficient quantity of beta-amylase in the digest to eliminate the more rapidly reacting G4 formed from the G3. A K(m) value of 9.4 +/- 0.8 mM for G3 was calculated from the data by a nonlinear least-squares method. Kinetic parameters for a series of higher malto-oligosaccharides (G4-G8) were also determined in both the synthetic and the phosphorolytic directions. A large change in the values of K(m) and V/e was seen on going from G3 to G4 for the synthetic reaction, and from G4 to G5 for the phosphorolytic. For the higher saccharides the V/e values do not vary strongly with increasing d.p., while the K(m) values tend to decrease, as has seen in the reactions of other plant phosphorylases.

  DOI：

  10.1016/0008-6215(91)84131-w
• 作为产物：
  描述：

  Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a1-4)a-Glc 在 sodium dihydrogenphosphate 作用下， 以 水 为溶剂， 生成 maltoheptaose
  参考文献：
  名称：

  Determination of kinetic parameters for maltotriose and higher malto-oligosaccharides in the reactions catalyzed by α-d-glucan phosphorylase from potato

  摘要：

  For kinetic studies on its synthetic and phosphorolytic reactions, alpha-D-glucan phosphorylase form potatoes was purified chromatographically until free of D-enzyme. Purified maltotriose (G3) is a poor primer in the phosphorylase-catalyzed synthetic reaction, showing an anomalous time course and making previous attempts to determine its kinetic parameters unsuccessful. In the present work the true rate of the G3-primed reaction was obtained from linear plots obtained by incorporating a sufficient quantity of beta-amylase in the digest to eliminate the more rapidly reacting G4 formed from the G3. A K(m) value of 9.4 +/- 0.8 mM for G3 was calculated from the data by a nonlinear least-squares method. Kinetic parameters for a series of higher malto-oligosaccharides (G4-G8) were also determined in both the synthetic and the phosphorolytic directions. A large change in the values of K(m) and V/e was seen on going from G3 to G4 for the synthetic reaction, and from G4 to G5 for the phosphorolytic. For the higher saccharides the V/e values do not vary strongly with increasing d.p., while the K(m) values tend to decrease, as has seen in the reactions of other plant phosphorylases.

  DOI：

  10.1016/0008-6215(91)84131-w

文献信息

• Characterization and mechanism of action of Microbacterium imperiale glucan 1,4-α-maltotriohydrolase
  作者：Chunsen Wu、Xing Zhou、Yan Xu、Hongyan Li、Yaoqi Tian、Xueming Xu、Zhengyu Jin

  DOI：10.1016/j.carres.2013.11.014

  日期：2014.1

  In this study, glucan 1,4-alpha-maltotriohydrolase (AMTS) from Microbacterium imperiale was purified and characterized. Hydrolysis by AMTS was affected by starch structure (e. g., amylose versus amylopectin) and hydrolysis time. During the initial phase of hydrolysis of maltooligosaccharides (G4-G7), AMTS displayed a unique transfer specificity to the transfer of maltotriosyl units. After extensive hydrolysis, maltotriose became the major end product, followed by glucose and maltose. Maltotetraose (G4) was the smallest donor in transglycosylation reactions by AMTS. This is the first study that reports transglycosylation activity of AMTS on maltooligosaccharides. The results of this study suggest that high purity maltotriose can be produced by the hydrolytic action of AMTS on starch. (C) 2013 Elsevier Ltd. All rights reserved.
• Site-Selective Glycosylation of Hemoglobin with Variable Molecular Weight Oligosaccharides: Potential Alternative to PEGylation
  作者：Thomas J. Styslinger、Ning Zhang、Veer S. Bhatt、Nicholas Pettit、Andre F. Palmer、Peng G. Wang

  DOI：10.1021/ja300893t

  日期：2012.5.2

  Poly(ethylene glycol) (PEG) conjugation (i.e., PEGylatiori) is a commonly used strategy to increase the circulatory half-life of therapeutic proteins and colloids; however, few viable alternatives exist to replicate its functions. Herein, we report a method for the rapid site-selective glycosylation of proteins with variously sized carbohydrates, up to a molecular weight (MW) of 10 000, thus serving as a potential alternative for PEGylation. More importantly, the method developed has two unique features. First, traditional protecting group strategies that typically accompany the modification of the carbohydrate fragments are circumvented, allowing for the facile site-selective glycosylation of a desired protein with variously sized glycans. Second, the methodology employed is not limited by oligosaccharide size; consequently, glycans of MW similar to that of PEG, used in the PEGylation of therapeutic proteins, can be employed. To demonstrate the usefulness of this technology, hemoglobin (Hb) was site-selectively glycosylated with a series of carbohydrates of increasing MW (from 504 to similar to 10 000). Hb was selected on the basis of the vast wealth of biochemical and biophysical knowledge present in the literature and because of its use as a precursor in the synthesis/formulation of artificial red blood cell substitutes. Following the successful site-selective glycosylation of Hb, the impact of increasing the glycan MW on Hb's biophysical properties was investigated in vitro.
• 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.
• Determination of kinetic parameters for maltotriose and higher malto-oligosaccharides in the reactions catalyzed by α-d-glucan phosphorylase from potato
  作者：Toshihiko Suganuma、Jun-Ichiro Kitazono、Kazuhiro Yoshinaga、Shigeo Fujimoto、Tomonori Nagahama

  DOI：10.1016/0008-6215(91)84131-w

  日期：1991.9

  For kinetic studies on its synthetic and phosphorolytic reactions, alpha-D-glucan phosphorylase form potatoes was purified chromatographically until free of D-enzyme. Purified maltotriose (G3) is a poor primer in the phosphorylase-catalyzed synthetic reaction, showing an anomalous time course and making previous attempts to determine its kinetic parameters unsuccessful. In the present work the true rate of the G3-primed reaction was obtained from linear plots obtained by incorporating a sufficient quantity of beta-amylase in the digest to eliminate the more rapidly reacting G4 formed from the G3. A K(m) value of 9.4 +/- 0.8 mM for G3 was calculated from the data by a nonlinear least-squares method. Kinetic parameters for a series of higher malto-oligosaccharides (G4-G8) were also determined in both the synthetic and the phosphorolytic directions. A large change in the values of K(m) and V/e was seen on going from G3 to G4 for the synthetic reaction, and from G4 to G5 for the phosphorolytic. For the higher saccharides the V/e values do not vary strongly with increasing d.p., while the K(m) values tend to decrease, as has seen in the reactions of other plant phosphorylases.