O-α-D-glucopyranosyl-(1->4)-α-D-glucopyranosyl α-D-glucopyranoside

• 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)-α-D-glucopyranosyl α-D-glucopyranoside
• 英文别名: 1,4-α-D-glucopyranosyl-[1,2-α-D-glucopyranosyl]-D-glucose；2,4-di-O-(α-D-glucopyranosyl)-D-glucopyranose；centose；Glc(a1-2)[Glc(a1-4)]b-Glc；(2R,3R,4S,5S,6R)-2-[(2R,3S,4S,5R,6R)-4,6-dihydroxy-2-(hydroxymethyl)-5-[(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol
• 化学式: C₁₈H₃₂O₁₆
• 分子量: 504.442
• InChiKey: GRDHQWBQPQWUOG-PVBPHLOOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -6.3
• 重原子数：
  34
• 可旋转键数：
  7
• 环数：
  3.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  269
• 氢给体数：
  11
• 氢受体数：
  16

反应信息

• 作为产物：
  描述：

  麦芽糖 在 schwanniomyces occidentalis α-glucosidase (SOG), mutant with Trp324 substituted by Tyr; W324Y 、 Rhizopus sp. glucoamylase 作用下， 以 aq. acetate buffer 为溶剂， 反应 5.0h， 生成 1,4-α-D-glucopyranosyl-[1,2-α-D-glucopyranosyl]-D-glucose 、 O-α-D-glucopyranosyl-(1->4)-α-D-glucopyranosyl α-D-glucopyranoside
  参考文献：
  名称：

  Aromatic Residue on β→α Loop 1 in the Catalytic Domain Is Important to the Transglycosylation Specificity of Glycoside Hydrolase Family 31 α-Glucosidase

  摘要：

  糖苷水解酶家族 31 种α-葡萄糖苷酶对α-1,4-和α-1,6-葡萄糖苷链的特异性各不相同。底物特异性的这种差异被认为是由于催化结构域β→α环 1 上的芳香残基具有（β/α）8 桶折叠的差异造成的；也就是说，β→α环 1 上具有 Tyr 和 Trp 的酶分别被称为α-1,4 特异性α-葡萄糖苷酶和α-1,6 特异性α-葡萄糖苷酶。然而，尽管西瓜酵母菌的α-葡萄糖苷酶在相应的位置上具有 Trp324，但它更喜欢α-1,4-葡萄糖苷键。将 Trp324 突变为 Tyr 会降低水解α-1,6-葡糖苷键和在转糖基化过程中形成α-1,6-葡糖苷键的能力，这表明 Trp324 与α-1,6 特异性密切相关，即使该酶更喜欢α-1,4-葡糖苷键。研究发现，与野生型酶相比，突变体酶催化生成支链寡糖--2,4-二-O-（α-d-吡喃葡萄糖基）-d-吡喃葡萄糖的效率更高。

  DOI：

  10.1271/bbb.130325

文献信息

• Identification of Bacillus selenitireducens MLS10 maltose phosphorylase possessing synthetic ability for branched α-d-glucosyl trisaccharides
  作者：Takanori Nihira、Yuka Saito、Motomitsu Kitaoka、Ken’ichi Otsubo、Hiroyuki Nakai

  DOI：10.1016/j.carres.2012.07.014

  日期：2012.10

  We discovered an inverting maltose phosphorylase (Bsel2056) belonging to glycoside hydrolase family 65 from Bacillus selenitireducens MLS10, which possesses synthetic ability for alpha-D-glucosyl disaccharides and trisaccharides through the reverse phosphorolysis with beta-D-glucose 1-phosphate as the donor. Bsel2056 showed the flexibility for monosaccharide acceptors with alternative C2 substituent (2-amino-2-deoxy-D-glucose, 2-deoxy-D-arabino-hexose, 2-acetamido-2-deoxy-D-glucose, D-mannose), resulting in production of 1,4-alpha-D-glucosyl disaccharides with strict regioselectivity. In addition, Bsel2056 synthesized two maltose derivatives possessing additional D-glucosyl residue bound to C2 position of the D-glucose residue at the reducing end, 1,4-alpha-D-glucopyranosyl-[1,2-alpha-D-glucopyranosyl]-D-glucose and 1,4-alpha-D-glucopyranosyl-[1,2-beta-D-glucopyranosyl]-D-glucose, from 1,2-alpha-D-glucopyranosyl-D-glucose (kojibiose) and 1,2-beta-D-glucopyranosyl-D-glucose (sophorose), respectively, as the acceptors. These results suggested that Bsel2056 possessed a binding space to accommodate the bulky C2 substituent of D-glucose. (C) 2012 Elsevier Ltd. All rights reserved.
• Aromatic Residue on β→α Loop 1 in the Catalytic Domain Is Important to the Transglycosylation Specificity of Glycoside Hydrolase Family 31 α-Glucosidase
  作者：Kyung-Mo SONG、Masayuki OKUYAMA、Mariko NISHIMURA、Takayoshi TAGAMI、Haruhide MORI、Atsuo KIMURA

  DOI：10.1271/bbb.130325

  日期：2013.8.23

  The specificity for the α-1,4- and α-1,6-glucosidic linkages varies among glycoside hydrolase family 31 α-glucosidases. This difference in substrate specificity has been considered to be due to the difference in an aromatic residue on β→α loop 1 in the catalytic domain with a (β/α)8 barrel fold; i.e., the enzymes having Tyr and Trp on β→α loop 1 were respectively described as α-1,4-specific and α-1,6-specific α-glucosidases. Schwanniomyces occidentalis α-glucosidase, however, prefers the α-1,4-glucosidic linkage, although the enzyme possesses Trp324 at the corresponding position. The mutation of Trp324 to Tyr decreased the ability for hydrolysis of the α-1,6-glucosidic linkage and formation of the α-1,6-glucosidic linkage in transglycosylation, indicating Trp324 to be closely associated with α-1,6 specificity, even if the enzyme preferred the α-1,4-glucosidic linkage. The mutant enzyme was found to catalyze the production of the branched oligosaccharide, 2,4-di-O-(α-d-glucopyranosyl)-d-glucopyranose, more efficiently than the wild-type enzyme.

  糖苷水解酶家族 31 种α-葡萄糖苷酶对α-1,4-和α-1,6-葡萄糖苷链的特异性各不相同。底物特异性的这种差异被认为是由于催化结构域β→α环 1 上的芳香残基具有（β/α）8 桶折叠的差异造成的；也就是说，β→α环 1 上具有 Tyr 和 Trp 的酶分别被称为α-1,4 特异性α-葡萄糖苷酶和α-1,6 特异性α-葡萄糖苷酶。然而，尽管西瓜酵母菌的α-葡萄糖苷酶在相应的位置上具有 Trp324，但它更喜欢α-1,4-葡萄糖苷键。将 Trp324 突变为 Tyr 会降低水解α-1,6-葡糖苷键和在转糖基化过程中形成α-1,6-葡糖苷键的能力，这表明 Trp324 与α-1,6 特异性密切相关，即使该酶更喜欢α-1,4-葡糖苷键。研究发现，与野生型酶相比，突变体酶催化生成支链寡糖--2,4-二-O-（α-d-吡喃葡萄糖基）-d-吡喃葡萄糖的效率更高。