p-nitrophenyl-β-D-glucopyranosyl-(1→6)-O-α-D-glucopyranoside

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: p-nitrophenyl-β-D-glucopyranosyl-(1→6)-O-α-D-glucopyranoside
• 英文别名: p-nitrophenyl β-D-isomaltoside；4-Nitrophenyl 6-o-(a-D-glucopyranosyl)-b-D-glucopyranoside；(2R,3S,4S,5R,6S)-2-(hydroxymethyl)-6-[[(2R,3S,4S,5R,6S)-3,4,5-trihydroxy-6-(4-nitrophenoxy)oxan-2-yl]methoxy]oxane-3,4,5-triol
• 化学式: C₁₈H₂₅NO₁₃
• 分子量: 463.395
• InChiKey: ISCYUJSLZREARS-GSPJEIBNSA-N

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：

  4-硝基苯-Β-D-吡喃葡萄糖苷 、 麦芽糖 在 Arthrobacter sp. DL001 α-D-glucoside glucohydrolase 作用下， 反应 0.5h， 生成 4-硝基苯基-Β-D-麦牙糖苷 、 p-nitrophenyl-β-D-glucopyranosyl-(1→6)-O-α-D-glucopyranoside
  参考文献：
  名称：

  Isolation and characterization of a novel α-glucosidase with transglycosylation activity from Arthrobacter sp. DL001

  摘要：

  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.

  DOI：

  10.1016/j.molcatb.2012.04.016

文献信息

• Environmentally benign glycosylation of aryl pyranosides and aryl/alkyl furanosides demonstrating the versatility of thermostable CGTase from Thermoanaerobacterium sp.
  作者：Alizé Pennec、Laurent Legentil、Luis Herrera-Estrella、Vincent Ferrières、Anne-Laure Chauvin、Caroline Nugier-Chauvin

  DOI：10.1039/c4gc00631c

  日期：——

  The specificity of transglycosylation of Thermoanaerobacterium sp. CGTase against aryl furanosides is reported.

  报道了Thermoanaerobacterium sp. CGTase对芳基呋喃苷的转糖基特异性。
• Acceptor-induced modification of regioselectivity in CGTase-catalyzed glycosylations of p-nitrophenyl-glucopyranosides
  作者：Simon Strompen、Alfonso Miranda-Molina、Agustín López-Munguía、Edmundo Castillo、Gloria Saab-Rincón

  DOI：10.1016/j.carres.2014.11.010

  日期：2015.3

  transfer reactions besides showing low hydrolytic activity. Here, the effect of the anomeric configuration of the glycosyl acceptor on the regioselectivity of CGTase catalyzed glycosylations was investigated. For this purpose, the α and β anomers of p-nitrophenyl-D-glucopyranoside were used as glycosyl acceptors, Bacillus macerans and Thermoanaerobacter sp. CGTases were used as biocatalysts and β-cyclodextrin

  据报道，环糊精糖基转移酶（CGTase）除了表现出低的水解活性外，还可以选择性催化α（1→4）-糖基转移反应。在此，研究了糖基受体的异头构型对CGTase催化的糖基化区域选择性的影响。为此，将对硝基苯基-D-吡喃葡萄糖苷的α和β端基异构体用作糖基受体，Macerans芽孢杆菌和Thermoanaerobacter sp.。CGTase被用作生物催化剂，β-环糊精被用作糖基供体。如所预期的，当将对硝基苯基-α-D-吡喃葡萄糖苷与豆腐芽孢杆菌CGTase用作受体时，产生了对硝基苯基-α-D-吡喃葡萄糖基-（1→4）-O-α-D-吡喃葡萄糖苷。令人惊讶的是，当使用对硝基苯基-β-D-吡喃葡萄糖苷作为糖基受体时，除了预期的α（1→4）-糖基化产物外，还获得了α（1→3）-和α（1→6）-转移产物。还观察到嗜热厌氧菌sp.macerans CGTase区域选择性的这种意想不到的变化，导致α（1→4）
• 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.