D-maltohexaose | 1184-46-9

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: D-maltohexaose
• 英文别名: maltohexaose；maltohexose；Maltohexanose, DP6；(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,3S,4R,5R)-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-6-(hydroxymethyl)oxane-3,4,5-triol
• CAS: 1184-46-9
• 化学式: C₃₆H₆₂O₃₁
• 分子量: 990.87
• InChiKey: OCIBBXPLUVYKCH-LIGGPISVSA-N

物化性质

• 沸点：
  1307.8±65.0 °C(Predicted)
• 密度：
  1.87±0.1 g/cm3(Predicted)
• 碰撞截面：
  279.7 Ų [M+Na]+ [CCS Type: DT, Method: stepped-field]

计算性质

• 辛醇/水分配系数(LogP)：
  -13.3
• 重原子数：
  67
• 可旋转键数：
  16
• 环数：
  6.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  506
• 氢给体数：
  20
• 氢受体数：
  31

反应信息

• 作为反应物：
  描述：

  D-maltohexaose 在 α-D-glucoside glucohydrolase EC 3.2.1.20 、 NaOAc buffer 作用下， 反应 30.0h， 生成 葡萄糖
  参考文献：
  名称：

  来自发芽小米种子的α-葡萄糖苷酶的纯化和表征

  摘要：

  摘要 α-葡萄糖苷酶（α-d-葡萄糖苷葡萄糖水解酶，EC 3.2.1.20）通过硫酸铵分馏、CM-cellulofine/Fractogel EMD SO 3 色谱法从发芽的小米（Panicum miliaceum L.）种子中分离出来。 Sephacryl S-200 HR 和 TSK 凝胶 Phenyl-5 PW，以及制备等电聚焦。该酶通过 SDS-PAGE 是同质的。根据其在 SDS-PAGE 中的迁移率估计该酶的分子量为 86,000，根据 TSKgel super SW 3000 的凝胶过滤估计为 80,000，这表明它由单个单元组成。该酶的等电点为8.3。该酶容易水解麦芽糖、麦芽低聚糖和 α-1,4-葡聚糖，但水解多糖的速度比麦芽糖快。K m 值随着底物分子量的增加而降低。麦芽七糖的值比麦芽糖的值低约 4 倍。该酶优选水解淀粉中的支链淀粉，但也容易水解具有α-1,3-糖苷键且在

  DOI：

  10.1016/j.phytochem.2005.02.024
• 作为产物：
  描述：

  α-环糊精 在 Pyrococcus furiosus thermostable amylase 作用下， 以 acetate buffer 为溶剂， 生成 D-maltohexaose
  参考文献：
  名称：

  Enzymatic preparation of maltohexaose, maltoheptaose, and maltooctaose by the preferential cyclomaltooligosaccharide (cyclodextrin) ring-opening reaction of Pyrococcus furiosus thermostable amylase

  摘要：

  Specific-length maltooligosaccharides, particularly maltohexaose, maltoheptaose, and maltooctaose, were prepared from cyclomaltooligosaccharides (cyclodextrins, CDs) by the preferential cyclodextrin ring-opening reaction of art amylolytic enzyme from Pyrococcus furiosus. The enzyme primarily produces maltohexaose, maltoheptaose, and maltooctaose by hydrolyzing alpha-, beta-, and gamma-CD, respectively. This study aims to develop a high-efficiency synthesis of specific maltooligosaccharides at high-purity.alpha-/beta-/gamma-cyclodextrins -> maltohexaose/maltoheptaose/maltooctaoseenzymaticring-opening reaction(c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2005.11.031

文献信息

• Regenerative labeling of saccharides
  作者：Hao-Yu Wen、Peng-Hao Hsu、Guei-San Chen、Jim-Min Fang

  DOI：10.1039/c3ra41426d

  日期：——

  A simple method for regenerative labeling of saccharides is devised by using (naphth-2-ylmethoxy)amine or N-methyl-(naphth-2-ylmethoxy)amine. The naphthyl group is optically responsive to facilitate the separation of labeled saccharides, which are subsequently reverted to the parental saccharides by one-pot hydrogenolysis–hydrolysis using co-catalysts Pd(OH)2 and HCl under an atmosphere of H2. The mechanistic study indicates that the naphthylmethyl group plays an essential role in the initial hydrogenolysis, followed by in situ hydrolysis, to regenerate the saccharides.

  设计了一种利用(萘-2-基甲氧基)胺或N-甲基-(萘-2-基甲氧基)胺对糖类进行再生标记的简单方法。萘基团具有光学响应性，有助于分离标记的糖类，这些糖类随后通过在H2气氛下使用共催化剂Pd(OH)2和HCl进行一步氢解-水解反应，还原为其母体糖类。机理研究表明，萘甲基团在初始氢解中起着至关重要的作用，随后进行原位水解，以再生糖类。
• Purification and Characterization of a Novel Fungal α-Glucosidase from<i>Mortierella alliacea</i>with High Starch-hydrolytic Activity
  作者：Yoshio TANAKA、Tsunehiro AKI、Yûki HIDAKA、Yûji FURUYA、Seiji KAWAMOTO、Seiko SHIGETA、Kazuhisa ONO、Osamu SUZUKI

  DOI：10.1271/bbb.66.2415

  日期：2002.1

  The fungal strain Mortierella alliacea YN-15 is an arachidonic acid producer that assimilates soluble starch despite having undetectable α-amylase activity. Here, a α-glucosidase responsible for the starch hydrolysis was purified from the culture broth through four-step column chromatography. Maltose and other oligosaccharides were less preferentially hydrolyzed and were used as a glucosyl donor for transglucosylation by the enzyme, demonstrating distinct substrate specificity as a fungal α-glucosidase. The purified enzyme consisted of two heterosubunits of 61 and 31 kDa that were not linked by a covalent bond but stably aggregated to each other even at a high salt concentration (0.5 M), and behaved like a single 92-kDa component in gel-filtration chromatography. The hydrolytic activity on maltose reached a maximum at 55°C and in a pH range of 5.0-6.0, and in the presence of ethanol, the transglucosylation reaction to form ethyl-α-D-glucoside was optimal at pH 5.0 and a temperature range of 45-50°C.

  真菌菌株Mortierella alliacea YN-15是一种能利用可溶性淀粉生产花生四烯酸的菌株，尽管其α-淀粉酶活性无法检测到。在此，通过四步柱层析从培养液中纯化出一种负责淀粉水解的α-葡萄糖苷酶。该酶对麦芽糖和其他低聚糖的水解优先性较低，但能将其作为葡萄糖供体进行转葡萄糖基作用，显示出作为真菌α-葡萄糖苷酶的独特底物特异性。纯化的酶由两个分别为61和31 kDa的异亚基组成，它们之间没有通过共价键连接，但在高盐浓度（0.5 M）下稳定地聚集在一起，在凝胶过滤层析中表现出如同一个92 kDa组分的特性。该酶对麦芽糖的水解活性在55°C和pH 5.0-6.0范围内达到最大，并且在存在乙醇的情况下，形成乙基-α-D-葡萄糖苷的转葡萄糖基反应在pH 5.0和温度范围45-50°C时最优。
• Synthesis of 1,3-di-O-alkyl-2-O-(β-glycosyl)glycerols bearing oligosaccharides as hydrophilic groups
  作者：Hiroyuki Minamikawa、Teiichi Murakami、Masakatsu Hato

  DOI：10.1016/0009-3084(94)90094-9

  日期：1994.8

  five steps via trichloroacetimidate glycosylation with 1,3-di-O-alkylglycerols. This route was applied to prepare the glycolipids bearing a cello- or malto-oligosaccharide with a definite number of sugar residues from one to six. Thin-layer chromatography, elemental analysis, nuclear magnetic resonance spectroscopy and infrared absorption spectroscopy confirmed that these glycolipids were chemically pure

  提出了一系列新的合成糖脂，1,3-二-O-烷基-2-O-（β-糖基）甘油及其有效合成途径。这些甘油糖脂通过三氯乙酰亚氨酸酯与1,3-二-O-烷基甘油的糖基化反应以五步合成，具有良好的总收率和立体选择性。该方法用于制备带有纤维寡糖或麦芽寡糖的糖脂，其中糖残基的数目为一到六个。薄层色谱法，元素分析，核磁共振谱和红外吸收谱证实，这些糖脂是化学纯的化合物。
• Synthesis of sulfated alkyl malto- and laminara-oligosaccharides with potent inhibitory effects on AIDS virus infection
  作者：Kaname Katsuraya、Naoya Ikushima、Nahoko Takahashi、Tadao Shoji、Hideki Nakashima、Naoki Yamamoto、Takashi Yoshida、Toshiyuki Uryu

  DOI：10.1016/0008-6215(94)80021-9

  日期：1994.7

  A series of sulfated alkyl oligosaccharides, including a sulfate dodecyl laminarapentaoside and a sulfated octadecyl maltohexaoside with potent anti-human immunodeficiency virus (HIV) activity, has been synthesized. An alkyl oligosaccharide in which a long alkyl group is bonded to the reducing end of the oligosaccharide was first synthesized in high yield. Peracetylated oligosaccharides reacted with

  合成了一系列硫酸化的烷基寡糖，包括具有有效抗人免疫缺陷病毒（HIV）活性的硫酸化十二烷基十二烷基戊糖苷和硫酸化十八烷基麦芽六糖苷。首先以高收率合成了其中长烷基键合至寡糖的还原端的烷基寡糖。过乙酰化的低聚糖与路易斯酸作为催化剂的脂肪族醇（如1-癸基醇和1-十二烷基醇）反应。如在α和β过乙酰化的糖苷的糖基化中一样，β异头异构体仅反应，在高温下用乙酸钠-乙酸酐进行乙酰化以使β异头异构体的比例最大化。
• Purification, Characterization, and Subsite Affinities of<i>Thermoactinomyces vulgaris</i>R-47 Maltooligosaccharide-metabolizing Enzyme Homologous to Glucoamylases
  作者：Kazuhiro ICHIKAWA、Takashi TONOZUKA、Rie UOTSU-TOMITA、Hiromi AKEBOSHI、Atsushi NISHIKAWA、Yoshiyuki SAKANO

  DOI：10.1271/bbb.68.413

  日期：2004.1

  A maltooligosaccharide-metabolizing enzyme from Thermoactinomyces vulgaris R-47 (TGA) homologous to glucoamylases does not degrade starch efficiently unlike most glucoamylases such as fungal glucoamylases (Uotsu-Tomita et al., Appl. Microbiol. Biotechnol., 56, 465–473 (2001)). In this study, we purified and characterized TGA, and determined the subsite affinities of the enzyme. The optimal pH and temperature of the enzyme are 6.8 and 60°C, respectively. Activity assays with 0.4% substrate showed that TGA was most active against maltotriose, but did not prefer soluble starch. Kinetic analysis using maltooligosaccharides ranging from maltose to maltoheptaose revealed that TGA has high catalytic efficiency for maltotriose and maltose. Based on the kinetics, subsite affinities were determined. The A1+A2 value of this enzyme was highly positive whereas A4–A6 values were negative and little affinity was detected at subsites 3 and 7. Thus, the subsite structure of TGA is different from that of any other GA. The results indicate that TGA is a metabolizing enzyme specific for small maltooligosaccharides.

  来自热活性放线菌（Thermoactinomyces vulgaris R-47，简称 TGA）的一个代谢小麦糊精酶与葡萄糖淀粉酶同源，但其降解淀粉的效率不如大多数葡萄糖淀粉酶，例如真菌葡萄糖淀粉酶（Uotsu-Tomita 等，应用微生物和生物技术，56，465–473（2001））。在这项研究中，我们纯化并表征了 TGA，并确定了该酶的亚位点亲和力。该酶的最佳 pH 值和温度分别为 6.8 和 60°C。0.4% 底物的活性测定表明，TGA 对麦三糖的活性最高，但对可溶性淀粉并不偏好。使用从麦芽糖到麦七糖的麦糊精进行的动力学分析显示，TGA 对麦三糖和麦芽糖具有很高的催化效率。基于动力学，确定了亚位点亲和力。该酶的 A1+A2 值高度正值，而 A4–A6 值为负值，在亚位点 3 和 7 上几乎没有检测到亲和力。因此，TGA 的亚位点结构与任何其他葡萄糖淀粉酶不同。结果表明，TGA 是一种特定于小麦糊精的代谢酶。