2-chloro-4-nitrophenol-α-D-maltotrioside

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 2-chloro-4-nitrophenol-α-D-maltotrioside
• 英文别名: 2-chloro-4-nitrophenyl α-D-maltotrioside；2-chloro-4-nitrophenyl-α-D-maltotrioside；2-chloro-p-nitrophenyl α-D-maltotrioside；2-chloro-p-nitrophenyl-α-D-maltotrioside；2-chloro-4-nitrophenyl α-maltotrioside；2-chloro-4-nitrophenylmaltotrioside；2-Chloro-4-nitrophenyl a-D-maltotrioside；(2R,3R,4S,5S,6R)-2-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-6-(2-chloro-4-nitrophenoxy)-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
• 化学式: C₂₄H₃₄ClNO₁₈
• 分子量: 659.983
• InChiKey: KMYYNUOXSFGLNX-XFNLHOCBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.1
• 重原子数：
  44
• 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：

  2-chloro-4-nitrophenol-α-D-maltotrioside 在 acetate buffer 、 α-amylase from Shochu Koji (aspergillus kawachii) 作用下， 以 水 为溶剂， 生成 直链淀粉 、 2-氯-4-硝基苯酚
  参考文献：
  名称：

  Distinguishable Action between Acid-stable and Neutral α-Amylases fromShochu Koji(Aspergillus kawachii)

  摘要：

  从烧酒麴（A. kawachii）中纯化了酸性稳定（KAA）和中性（KNA）α-淀粉酶，并研究了它们对麦芽寡糖的作用。KAA 与 KNA 可通过以下作用进行区分：在 KAA 作用下，麦芽戊糖（G5）会优先水解第三个苷键，而硫氰酸钾（KSCN）的加入会降低 2-氯-4-硝基苯基-α-麦芽三糖苷（CNP-G3）的 CNP 释放率。

  DOI：

  10.1271/bbb.61.1617

文献信息

• Synthesis and characterisation of novel chromogenic substrates for human pancreatic α-amylase
  作者：Iben Damager、Shin Numao、Hongming Chen、Gary D Brayer、Stephen G Withers

  DOI：10.1016/j.carres.2004.05.019

  日期：2004.7

  maltose and maltotriose were chemically synthesised as substrates for human pancreatic α-amylases and subjected to kinetic analysis. Rates measured were shown to reflect both hydrolysis and transglycosylation reactions. 4-O-Methylated derivatives of these substrates underwent only hydrolysis, thereby simplifying kinetic analyses. These modified substrates may be used for the detection and kinetic analysis

  化学合成麦芽糖和麦芽三糖的衍生物作为人胰腺α-淀粉酶的底物，并进行动力学分析。已显示测得的速率反映了水解反应和转糖基化反应。这些底物的4-O-甲基化衍生物仅进行水解，从而简化了动力学分析。这些修饰的底物可用于α-淀粉酶的检测和动力学分析，可用于快速筛选新型α-淀粉酶抑制剂和随后的动力学表征。
• Study of the action of human salivary alpha-amylase on 2-chloro-4-nitrophenyl α-maltotrioside in the presence of potassium thiocyanate
  作者：Toshihiko Suganuma、Yoshiaki Maeda、Kanefumi Kitahara、Tomonori Nagahama

  DOI：10.1016/s0008-6215(97)00150-x

  日期：1997.9

  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.
• A New Nanobiocatalytic System Based on Allosteric Effect with Dramatically Enhanced Enzymatic Performance
  作者：Liang-Bing Wang、You-Cheng Wang、Rong He、Awei Zhuang、Xiaoping Wang、Jie Zeng、J. G. Hou

  DOI：10.1021/ja3120136

  日期：2013.1.30

  We report a rational design of CaHPO4-alpha-aamylase hybrid nanobiocatalytic system based on allosteric effect and an explanation of the increase in catalytic activity when certain enzymes are immobilized in specific nanomaterials. Employing a calcification approach in aqueous solutions, we acquired such new nanobiocatalytic systems with three different morphologies, i.e., nanoflowers, nanoplates, and parallel hexahedrons. Through studying enzymatic performance of these systems and free alpha-amylase with/without Ca2+, we demonstrated how two factors, allosteric regulation and morphology of the as-synthesized nanostructures, predominantly influence enzymatic activity. Benefiting from both the allosteric modulation and its hierarchical structure, CaHPO4-alpha-amylase hybrid nanoflowers exhibited dramatically enhanced enzymatic activity. As a bonus, the new system we devised was found to enjoy higher stability and durability than free alpha-amylase plus Ca2+.
• Distinguishable Action between Acid-stable and Neutral α-Amylases from<i>Shochu Koji</i>(<i>Aspergillus kawachii</i>)
  作者：Toshihiko Suganuma、Naoyuki Noda、Hiroyuki Honbo、Kanefumi Kitahara

  DOI：10.1271/bbb.61.1617

  日期：1997.1

  Acid-stable (KAA) and neutral (KNA) α-amylases from shochu koji (A. kawachii) were purified and their actions towards maltooligosaccharides were studied. KAA could be distinguished from KNA by the following actions: with KAA, maltopentaose (G5) was preferentially hydrolyzed at the third glycoside bond, and the addition of potassium thiocyanate (KSCN) decreased the rate of CNP-release from 2-chloro-4-nitrophenyl-α-maltotrioside (CNP-G3).

  从烧酒麴（A. kawachii）中纯化了酸性稳定（KAA）和中性（KNA）α-淀粉酶，并研究了它们对麦芽寡糖的作用。KAA 与 KNA 可通过以下作用进行区分：在 KAA 作用下，麦芽戊糖（G5）会优先水解第三个苷键，而硫氰酸钾（KSCN）的加入会降低 2-氯-4-硝基苯基-α-麦芽三糖苷（CNP-G3）的 CNP 释放率。