maltotetraosyltrehalose | 171609-69-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: maltotetraosyltrehalose
• 英文别名: Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a1-1a)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)-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-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol
• CAS: 171609-69-1
• 化学式: C₃₆H₆₂O₃₁
• 分子量: 990.87
• InChiKey: WHOZUKCKVDCMGF-DWJDYNGGSA-N

物化性质

• 沸点：
  1312.2±65.0 °C(Predicted)
• 密度：
  1.87±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -14.1
• 重原子数：
  67.0
• 可旋转键数：
  16.0
• 环数：
  6.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  506.13
• 氢给体数：
  20.0
• 氢受体数：
  31.0

反应信息

• 作为反应物：
  描述：

  maltotetraosyltrehalose 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：

  maltohexaose 在 maltooligosyltrehalose synthase F₂₀₆W mutant 作用下， 以 various solvent(s) 为溶剂， 生成 maltotetraosyltrehalose
  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

• Formation of Trehalose from Maltooligosaccharides by a Novel Enzymatic System
  作者：Kazuhiko Maruta、Tetsuya Nakada、Michio Kubota、Hiroto Chaen、Toshiyuki Sugimoto、Masashi Kurimoto、Yoshio Tsujisaka

  DOI：10.1271/bbb.59.1829

  日期：1995.1

  A trehalose-producing bacterium, Arthrobacter sp. strain Q36, was isolated from soil. From a supernatant of the culture broth, two novel enzymes related to trehalose synthesis were partially purified by Sepabeads FP-DA column chromatography. One enzyme catalyzed the conversion of maltopentaose into maltotriosyl trehalose by intramolecular transglycosylation, showing it to be maltooligosyl trehalose synthase. The other hydrolyzed the product transferred by the former into maltotriose and trehalose specifically, showing it to be maltooligosyl trehalose trehalohydrolase. In addition to the bacterial strain isolated, several bacteria kept in our laboratory were found to produce these enzymes. The enzymatic system was proposed to be a novel biosynthesis of trehalose in bacteria involving the following reactions: maltodextrin→maltooligosyl trehalose, maltooligosyl trehalose→maltodextrin + trehalose. When these enzymes acted on amylose simultaneously, the trehalose in the reaction mixture reached more than 80% in content.

  从土壤中分离出了一种产生曲哈糖的细菌--节杆菌 Q36 菌株。通过 Sepabeads FP-DA 柱色谱法，从培养液的上清液中部分纯化出两种与三卤糖合成有关的新型酶。一种酶通过分子内转糖基化催化麦芽酮戊糖转化为麦芽三糖，表明它是麦芽寡糖三糖合成酶。另一种则将前者转移的产物特异性地水解为麦芽三糖和曲哈糖，表明它是麦芽寡糖基曲哈糖曲哈水解酶。除了分离出的细菌菌株外，我们还发现实验室中的几种细菌也能产生这些酶。该酶系统被认为是细菌中一种新型的三卤糖生物合成方法，涉及以下反应：麦芽糊精→麦芽寡糖基三卤糖，麦芽寡糖基三卤糖→麦芽糊精+三卤糖。当这些酶同时作用于直链淀粉时，反应混合物中的三卤糖含量达到 80% 以上。
• 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.