4-硝基苯基-Β-麦芽三糖苷 | 66451-58-9

• 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-Β-麦芽三糖苷
• 英文名称: 4-nitrophenyl α-maltotrioside
• 英文别名: Glc(a1-4)Glc(a1-4)Glc(a)-O-Ph(4-NO2)；(2R,3R,4S,5S,6R)-2-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-4,5-dihydroxy-2-(hydroxymethyl)-6-(4-nitrophenoxy)oxan-3-yl]oxy-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol
• CAS: 66451-58-9
• 化学式: C₂₄H₃₅NO₁₈
• 分子量: 625.538
• InChiKey: BETIRLUWOMCBBJ-XFNLHOCBSA-N

物化性质

• 沸点：
  971.0±65.0 °C(Predicted)
• 密度：
  1.75±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -4.7
• 重原子数：
  43
• 可旋转键数：
  9
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  304
• 氢给体数：
  10
• 氢受体数：
  18

反应信息

• 作为反应物：
  描述：

  4-硝基苯基-Β-麦芽三糖苷 在 human salivary alpha-amylase 、 MES-buffer 、 sodium chloride 、 calcium chloride 作用下， 以 水 为溶剂， 反应 0.17h， 生成 对硝基苯酚 、 maltotriose
  参考文献：
  名称：

  Study of the action of human salivary alpha-amylase on 2-chloro-4-nitrophenyl α-maltotrioside in the presence of potassium thiocyanate

  摘要：

  The degradation mechanism of a synthetic substrate, 2-chloro-4-nitrophenyl alpha-maltotrioside (CNP-G(3)), by human salivary alpha-amylase (HSA) was investigated by kinetic and product analyses. It was observed that the enzyme attacked the various CNP-maltooligosaccharides (CNP-G(3) to CNP-G(6)) releasing free CNP. Addition of 500 mM potassium thiocyanate (KSCN) was also found to greatly increase the rates of CNP-release. It was the fastest with CNP-G(3), and, in the presence of KSCN, was almost comparable to that of degradation of maltopentaose (G(5)). On the other hand, addition of KSCN decreased the rate of cleavage between glucan-glucan bonds in maltopentaose. Product analysis showed that KSCN addition altered the cleavage distribution which occurred 100% at the bond between CNP and G(3), and that product distribution of free CNP was largely dependent on substrate concentration. Formation of CNP-G,, a larger product than the original substrate CNP-G,, was found to be present in the digest at high concentrations of substrate and in the presence of KSCN. Based on these results, a degradation pathway for CNP-G(3) involving transglycosylation besides direct hydrolysis is proposed. The increase of the CNP-release by the addition of KSCN would result from a corresponding increase in the interaction between the CNP moiety and the corresponding subsite near the catalytic site, as well as the enhancement of the catalytic efficiency. (C) 1997 Elsevier Science Ltd.

  DOI：

  10.1016/s0008-6215(97)00150-x
• 作为产物：
  描述：

  对硝基苯基麦芽五糖 在 α-淀粉酶,以淀粉稀释(来自枯草芽孢杆菌) 作用下， 以 水 为溶剂， 生成 对硝基苯基麦芽糖苷 、 4-硝基苯基-Β-麦芽三糖苷 、 对硝基苯-α-D-葡萄糖吡喃苷
  参考文献：
  名称：

  Synthesis of p-nitrophenyl 65-O-benzyl-α-maltopentaoside, a substrate for alpha amylases

  摘要：

  p-Nitrophenyl alpha-maltopentaoside, having a benzyl group on O-6 of the terminal (nonreducing) D-glucosyl group was prepared by use of a reductive ring-opening reaction. Highly regioselective reduction of p-nitrophenyl O-(2,3-di-O-benzoyl-4,6-O-benzylidene-alpha-D-glucopyranosyl)-(1----4)- tris[O-(2,3,6-tri-O-benzoyl-alpha-D-glucopyranosyl)-(1----4)]-2,3,6-tri- O- benzoyl-alpha-D-glucopyranoside by dimethylamine-borane and p-toluenesulfonic acid, followed by debenzoylation, gave p-nitrophenyl O-(6-O-benzyl-alpha-D-glucopyranosyl)-(1----4)-tris[O-alpha-D-glucopyran osyl- (1----4)]-alpha-D-glucopyranoside. An experiment was done on the mode of action of human pancreatic and salivary alpha amylases on this derivative. The compound is suitable as a substrate for the assay of alpha amylase when used with glucoamylase and alpha-D-glucosidase as coupling enzymes.

  DOI：

  10.1016/0008-6215(88)84062-x

文献信息

• 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）
• The action of germinated barley alpha-amylases on linear maltodextrins
  作者：Alex.W. MacGregor、Joan E. Morgan、E.Ann MacGregor

  DOI：10.1016/0008-6215(92)85080-j

  日期：1992.4

  The actions of barley alpha-amylase isozymes 1 and 2 (EC 3.2.1.1) on malto-oligosaccharides and their p-nitrophenyl glycosides were similar, but not identical. For each isozyme, transglycosylation occurred with small substrates that were hydrolysed with difficulty, whereas the rates of hydrolysis increased with increase in the size of the substrate for both the malto-oligosaccharides and the p-nitrophenyl glycosides. A p-nitrophenyl group was found to mimic a glucose residue to a large extent. The differences in action of the isozymes are believed to be caused by differences at more than one subsite of the active site. A lysine-arginine substitution is postulated to account for some of the observed variations.
• Ono, Mitsunori; Suzuki, Nobuo; Hirano, Shigeo, Chemistry Letters, 1991, # 3, p. 395 - 398
  作者：Ono, Mitsunori、Suzuki, Nobuo、Hirano, Shigeo、Itoh, Isamu、Masuta, Nobuhito

  DOI：——

  日期：——
• Modified malto-oligosaccharides as inhibitors of human alpha-amylases
  作者：Kaoru Omichi、Sumihiro Hase、Tokuji Ikenaka

  DOI：10.1016/0008-6215(90)80118-m

  日期：1990.12