O-(α-D-glucopyranosyl)-(1->4)-O-(α-D-glucopyranosyl)-(1->4)-O-(α-D-glucopyranosyl)-(1->4)-α-D-glucopyranosyl-α-D-glucopyranoside | 142831-49-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: O-(α-D-glucopyranosyl)-(1->4)-O-(α-D-glucopyranosyl)-(1->4)-O-(α-D-glucopyranosyl)-(1->4)-α-D-glucopyranosyl-α-D-glucopyranoside
• 英文别名: O-α-D-glucopyranosyl-(1->4)-O-α-D-glucopyranosyl-(1->4)-O-α-D-glucopyranosyl-(1->4)-α-D-glucopyranosyl α-D-glucopyranoside；maltotriosyltrehalose；G3T；(2R,3R,4S,5S,6R)-2-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-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: 142831-49-0
• 化学式: C₃₀H₅₂O₂₆
• 分子量: 828.727
• InChiKey: GUZBXMVHVQHCTQ-XFSSMLLMSA-N

物化性质

• 沸点：
  1181.3±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)：
  -10.6
• 重原子数：
  56
• 可旋转键数：
  13
• 环数：
  5.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  427
• 氢给体数：
  17
• 氢受体数：
  26

反应信息

• 作为反应物：
  描述：

  O-(α-D-glucopyranosyl)-(1->4)-O-(α-D-glucopyranosyl)-(1->4)-O-(α-D-glucopyranosyl)-(1->4)-α-D-glucopyranosyl-α-D-glucopyranoside 在 Sulfolobus solfataricus maltooligosyltrehalose trehalohydrolase 作用下， 以 aq. citrate phosphate buffer 为溶剂， 生成 海藻糖
  参考文献：
  名称：

  Identification of the Essential Catalytic Residues and Selectivity-Related Residues of Maltooligosyltrehalose Trehalohydrolase from the Thermophilic Archaeon Sulfolobus solfataricus ATCC 35092

  摘要：

  Maltooligosyltrehalose trehalohydrolase (MTHase) catalyzes the release of trehalose by cleaving the alpha-1,4-glucosidic linkage next to the alpha-1,1-linked terminal disaccharide of maltooligosyltrehalose. Mutations at residues D255, E286, and D380 were constructed to identify the essential catalytic residues of MTHase, while mutations at residues W218, A259, Y328, F355, and R356 were constructed to identify selectivity-related residues of the enzyme. The specific activities of the purified D255A, E286A, and D380A MTHases were only 0.15, 0.09 and 0.01%, respectively, of that of wildtype MTHase, suggesting that these three residues are essential catalytic residues. Compared with wild-type MTHase, A259S, Y328F, F355Y, and R356K MTHases had increased selectivity ratios, which were defined as the ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively, while W218A and W218F MTHases had decreased selectivity ratios. When starch digestion was carried out at 75 degrees C and wild-type and mutant MTHases were, respectively, used with isoamylase and maltooligosyltrehalose synthase (MTSase), the ratios of initial rates of glucose formation to those of trehalose formation were inversely correlated to the peak trehalose yields.

  DOI：

  10.1021/jf073320b
• 作为产物：
  描述：

  麦芽五糖 在 maltooligosyltrehalose synthase F₄₀₅M mutant 作用下， 以 various solvent(s) 为溶剂， 生成 O-(α-D-glucopyranosyl)-(1->4)-O-(α-D-glucopyranosyl)-(1->4)-O-(α-D-glucopyranosyl)-(1->4)-α-D-glucopyranosyl-α-D-glucopyranoside
  参考文献：
  名称：

  Protein Engineering of Sulfolobus solfataricus Maltooligosyltrehalose Synthase To Alter Its Selectivity

  摘要：

  Maltooligosyltrehalose synthase (MTSase) is one of the key enzymes involved in trehalose production from starch and catalyzes an intramolecular transglycosylation reaction by converting the alpha-1,4- to alpha,alpha-1,1-glucosidic linkage. Mutations at residues F206, F207, and F405 were constructed to change the selectivity of the enzyme because the changes in selectivity could reduce the side hydrolysis reaction of releasing glucose and thus increase trehalose production from starch. As compared with wild-type MTSase, F405Y and F405M MTSases had decreased ratios of the initial rate of glucose formation to that of trehalose formation in starch digestion at 75 degrees C when wild-type and mutant MTSases were, respectively, used with isoamylase and maltooligosyltrehalose trehalohydrolase (MTHase). The highest trehalose yield from starch digestion was by the mutant MTSase having the lowest initial rate of glucose formation to trehalose formation, and this predicted high trehalose yield better than the ratio of catalytic efficiency for hydrolysis to that for transglycosylation.

  DOI：

  10.1021/jf0701279

文献信息

• All-α-d-linked tetra- and penta-saccharide substructures of Trestatin A by block syntheses with triflic anhydride as promoter
  作者：Hans Peter Wessel、Beatrice Mayer、Gerhard Englert

  DOI：10.1016/0008-6215(93)80028-d

  日期：1993.4

  The perbenzylated maltosyl and maltotriosyl fluorides 6 and 16 were treated with 2,3,2',3',6'-penta-O-benzyl-4,6-O-benzylidene-alpha,alpha-trehalose (7) using triflic anhydride as a promoter to give all-alpha-D-linked tetra- and penta-saccharides which were finally deblocked to the free oligosaccharides 4-O-alpha-maltosyl- 9 and 4-O-alpha-maltotriosyl-alpha,alpha-trehaloses 18. The H-1 NMR spectra of some of the compounds were fully analyzed by 1D TOCSY and ROESY experiments.
• Mutations on Aromatic Residues of the Active Site To Alter Selectivity of the<i> Sulfolobus solfataricus</i> Maltooligosyltrehalose Synthase
  作者：Tsuei-Yun Fang、Wen-Chi Tseng、Yao-Te Chung、Ching-Hsing Pan

  DOI：10.1021/jf060152z

  日期：2006.5.1

  Mutations Y290F, Y367F, F405Y, and Y409F located near subsite + 1 were constructed in maltooligosyltrehalose synthase (MTSase) to alter the selectivity of the enzyme. These mutations were designed to evaluate the effects of hydrophobic interactions and/or hydrogen bondings on transglycosylation and side hydrolysis reactions. The catalytic efficiencies of Y290F MTSase for hydrolysis and transglycosylation reactions were only 6.6 and 5.6%, respectively, of those of wildtype MTSase, whereas the catalytic efficiencies of Y367F MTSase were decreased by about half. F405Y MTSase had similar catalytic efficiencies for transglycosylation and a somewhat lower catalytic efficiency for hydrolysis. Y409F MTSase had somewhat lower catalytic efficiencies for the transglycosylation and a similar catalytic efficiency for hydrolysis. Y290F and Y367F MTSases had large changes in (G), suggesting that there are hydrogen bonds between the substrate and residues Y290 and Y367 of wild-type MTSase. Compared with wild-type MTSase, F405Y MTSase had decreased ratios of hydrolysis to transglycosylation, whereas Y290F, Y367F, and Y409F MTSases had increased ratios. These results suggest that use of F405Y MTSase might result in a higher yield of trehalose production from starch when it replaces wild-type MTSase.
• Identification of the Essential Catalytic Residues and Selectivity-Related Residues of Maltooligosyltrehalose Trehalohydrolase from the Thermophilic Archaeon Sulfolobus solfataricus ATCC 35092
  作者：Tsuei-Yun Fang、Wen-Chi Tseng、Tong-Yuan Shih、Mei-Ying Wang

  DOI：10.1021/jf073320b

  日期：2008.7.1

  Maltooligosyltrehalose trehalohydrolase (MTHase) catalyzes the release of trehalose by cleaving the alpha-1,4-glucosidic linkage next to the alpha-1,1-linked terminal disaccharide of maltooligosyltrehalose. Mutations at residues D255, E286, and D380 were constructed to identify the essential catalytic residues of MTHase, while mutations at residues W218, A259, Y328, F355, and R356 were constructed to identify selectivity-related residues of the enzyme. The specific activities of the purified D255A, E286A, and D380A MTHases were only 0.15, 0.09 and 0.01%, respectively, of that of wildtype MTHase, suggesting that these three residues are essential catalytic residues. Compared with wild-type MTHase, A259S, Y328F, F355Y, and R356K MTHases had increased selectivity ratios, which were defined as the ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively, while W218A and W218F MTHases had decreased selectivity ratios. When starch digestion was carried out at 75 degrees C and wild-type and mutant MTHases were, respectively, used with isoamylase and maltooligosyltrehalose synthase (MTSase), the ratios of initial rates of glucose formation to those of trehalose formation were inversely correlated to the peak trehalose yields.
• Protein Engineering of <i>Sulfolobus solfataricus</i> Maltooligosyltrehalose Synthase To Alter Its Selectivity
  作者：Tsuei-Yun Fang、Wen-Chi Tseng、Ching-Hsing Pan、Yao-Te Chun、Mei-Ying Wang

  DOI：10.1021/jf0701279

  日期：2007.7.1

  Maltooligosyltrehalose synthase (MTSase) is one of the key enzymes involved in trehalose production from starch and catalyzes an intramolecular transglycosylation reaction by converting the alpha-1,4- to alpha,alpha-1,1-glucosidic linkage. Mutations at residues F206, F207, and F405 were constructed to change the selectivity of the enzyme because the changes in selectivity could reduce the side hydrolysis reaction of releasing glucose and thus increase trehalose production from starch. As compared with wild-type MTSase, F405Y and F405M MTSases had decreased ratios of the initial rate of glucose formation to that of trehalose formation in starch digestion at 75 degrees C when wild-type and mutant MTSases were, respectively, used with isoamylase and maltooligosyltrehalose trehalohydrolase (MTHase). The highest trehalose yield from starch digestion was by the mutant MTSase having the lowest initial rate of glucose formation to trehalose formation, and this predicted high trehalose yield better than the ratio of catalytic efficiency for hydrolysis to that for transglycosylation.