4-硝基苯基6-O-alpha-D-吡喃葡萄糖基-alpha-D-吡喃葡萄糖苷 | 72647-96-2

• 分子结构分类: 有机化合物 - 有机氧化合物
• 中文名称: 4-硝基苯基6-O-alpha-D-吡喃葡萄糖基-alpha-D-吡喃葡萄糖苷
• 中文别名: 吡咯烷,1-(2-氟-3-甲基-1-羰基戊基)-2,5-二甲基-,[2R-[1(2S*,3R*),2α,5β]]-(9CI)；1,6-氨基-2,3-二乙氧基-BET-D-赤藓基-己二-2-烯丙基
• 英文名称: 4-nitrophenyl α-isomaltoside
• 英文别名: 4-Nitrophenyl 6-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside；(2R,3S,4S,5R,6S)-2-(hydroxymethyl)-6-[[(2R,3S,4S,5R,6R)-3,4,5-trihydroxy-6-(4-nitrophenoxy)oxan-2-yl]methoxy]oxane-3,4,5-triol
• CAS: 72647-96-2；80321-98-8；104872-92-6；107870-85-9；131348-49-7；143615-14-9；144939-65-1；145772-76-5；136734-56-0
• 化学式: C₁₈H₂₅NO₁₃
• 分子量: 463.395
• InChiKey: ISCYUJSLZREARS-XCZSIQBNSA-N

物化性质

• 熔点：
  130-132°C
• 沸点：
  791.3±60.0 °C(Predicted)
• 密度：
  1.70±0.1 g/cm3(Predicted)
• 溶解度：
  溶于DMSO、甲醇、水

计算性质

• 辛醇/水分配系数(LogP)：
  -2.6
• 重原子数：
  32
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  224
• 氢给体数：
  7
• 氢受体数：
  13

反应信息

• 作为产物：
  描述：

  β-D-glucosyl fluoride 、 对硝基苯-α-D-葡萄糖吡喃苷 在 recombinant enzyme D₄₈₁G 作用下， 以 acetate buffer 为溶剂， 反应 1.33h， 以29%的产率得到对硝基苯基麦芽糖苷
  参考文献：
  名称：

  α-Glucosidase Mutant Catalyzes “α-Glycosynthase”-type Reaction

  摘要：

  用甘氨酸取代酿酒酵母菌 α-葡萄糖苷酶的催化亲核体 Asp481，可消除其水解活性。研究发现突变体酶（D481G）能催化β-葡萄糖酰氟和 4-硝基苯基（PNP）α-葡萄糖苷形成α-葡萄糖苷连接，生成两种 PNP α-二葡萄糖苷，即α-异麦芽糖苷和α-麦芽糖苷。这两种产物未被 D481G水解，PNP α-异麦芽糖苷和 α-麦芽糖苷的产量分别为 41% 和 29%。PNP 单糖苷（如 α-木糖苷、α-甘露糖苷或 β-葡萄糖苷）可作为底物，但 PNP α-半乳糖苷和麦芽糖不能。在 α-葡萄糖酰氟和 PNP α-葡萄糖苷的组合中，没有观察到可检测到的产物。这项研究首次报道了 "α-糖苷合成酶 "类型的形成α-糖苷键的反应。

  DOI：

  10.1271/bbb.66.928

文献信息

• Isolation and characterization of a novel α-glucosidase with transglycosylation activity from Arthrobacter sp. DL001
  作者：Kun Zhou、Hong-wei Luan、Ying Hu、Guang-bo Ge、Xing-bao Liu、Xiao-chi Ma、Jie Hou、Xiu-li Wang、Ling Yang

  DOI：10.1016/j.molcatb.2012.04.016

  日期：2012.8

  A strain of Arthrobacter sp. DL001 with high transglycosylation activity was successfully isolated from the Yellow Sea of China. To purify the extracellular enzyme responsible for transglycosylation, a four-step protocol was adopted and the enzyme with electrophoretical purity was obtained. The purified enzyme has a molecular mass of 210 kDa and displays a narrow hydrolysis specificity towards alpha-1,4-glucosidic bond. Its hydrolytic activity was identified as decreasing in the order of maltotriose > panose > maltose. Only 3.61% maltose activity occurs when p-nitrophenyl alpha-D-glycopyranoside serves as a substrate, suggesting that this enzyme belongs to the type II alpha-glucosidase. In addition, the enzyme was able to transfer glucosyl groups from the donors containing alpha-1,4-glucosidic bond specific to glucosides, xylosides and alkyl alcohols in alpha-1,4- or alpha-1,6-manners. A decreased order of activity was observed when maltose, maltotriose, panose, beta-cyclodextrin and soluble starch served as glycosyl donors, respectively. When maltose was utilized as a donor and a series of p-nitrophenyl-glycosides as acceptors, the glucosidase was capable of transferring glucosyl groups to p-nitrophenyl-glucosides and p-nitrophenyl-xylosides in alpha-1,4- or alpha-1,6-manners. The yields of p-nitrophenyl-oligosaccharides could reach 42-60% in 2 h. When a series of alkyl alcohols were utilized as acceptors, the enzyme exhibited its transglycosylation activities not only to the primary alcohols but also to the secondary alcohols with carbon chain length 1-4. Therefore, all the results indicated that the purified alpha-glucosidase present a useful tool for the biosynthesis of oligosaccharides and alkyl glucosides. (C) 2012 Elsevier B.V. All rights reserved.
• Enzymic synthesis of p-nitrophenyl α-glucobiosides by use of native and immobilized rice α-glucosidase
  作者：Naoki Asano、Ken Tanaka、Katsuhiko Matsui

  DOI：10.1016/0008-6215(91)84137-4

  日期：1991.9
• α-Glucosidase Mutant Catalyzes “α-Glycosynthase”-type Reaction
  作者：Masayuki OKUYAMA、Haruhide MORI、Kotomi WATANABE、Atsuo KIMURA、Seiya CHIBA

  DOI：10.1271/bbb.66.928

  日期：2002.1

  Replacement of the catalytic nucleophile Asp481 by glycine in Schizosaccharomyces pombe α-glucosidase eliminated the hydrolytic activity. The mutant enzyme (D481G) was found to catalyze the formation of an α-glucosidic linkage from β-glucosyl fluoride and 4-nitrophenyl (PNP) α-glucoside to produce two kinds of PNP α-diglucosides, α-isomaltoside and α-maltoside. The two products were not hydrolyzed by D481G, giving 41 and 29% yields of PNP α-isomaltoside and α-maltoside, respectively. PNP monoglycosides, such as α-xyloside, α-mannoside, or β-glucoside, acted as the substrate, but PNP α-galactoside and maltose could not. No detectable product was observed in the combination of α-glucosyl fluoride and PNP α-glucoside. This study is the first report on an “α-glycosynthase”-type reaction to form an α-glycosidic linkage.

  用甘氨酸取代酿酒酵母菌 α-葡萄糖苷酶的催化亲核体 Asp481，可消除其水解活性。研究发现突变体酶（D481G）能催化β-葡萄糖酰氟和 4-硝基苯基（PNP）α-葡萄糖苷形成α-葡萄糖苷连接，生成两种 PNP α-二葡萄糖苷，即α-异麦芽糖苷和α-麦芽糖苷。这两种产物未被 D481G水解，PNP α-异麦芽糖苷和 α-麦芽糖苷的产量分别为 41% 和 29%。PNP 单糖苷（如 α-木糖苷、α-甘露糖苷或 β-葡萄糖苷）可作为底物，但 PNP α-半乳糖苷和麦芽糖不能。在 α-葡萄糖酰氟和 PNP α-葡萄糖苷的组合中，没有观察到可检测到的产物。这项研究首次报道了 "α-糖苷合成酶 "类型的形成α-糖苷键的反应。