6-[6-(6-氨基己酰氨基)己酰氨基]己酸 | 5776-78-3

• 物质功能分类: 催化剂及助剂 - 聚合物
• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 中文名称: 6-[6-(6-氨基己酰氨基)己酰氨基]己酸
• 中文别名: 氨基己酸三聚体杂质
• 英文名称: 6-[6-(6-amino-hexanoylamino)-hexanoylamino]-hexanoic acid
• 英文别名: 6-[6-(6-Amino-hexanoylamino)-hexanoylamino]-hexansaeure；Hexanoic acid, 6-[[6-[(6-amino-1-oxohexyl)amino]-1-oxohexyl]amino]-；6-[6-(6-aminohexanoylamino)hexanoylamino]hexanoic acid
• CAS: 5776-78-3
• 化学式: C₁₈H₃₅N₃O₄
• 分子量: 357.494
• InChiKey: JOIUZBTWMAYEQW-UHFFFAOYSA-N

物化性质

• 熔点：
  218-220 °C
• 沸点：
  659.8±50.0 °C(Predicted)
• 密度：
  1.064±0.06 g/cm3(Predicted)
• 溶解度：
  可溶于酸性水溶液（轻微）、甲醇（轻微）、水（轻微）

计算性质

• 辛醇/水分配系数(LogP)：
  -1.8
• 重原子数：
  25
• 可旋转键数：
  17
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  122
• 氢给体数：
  4
• 氢受体数：
  5

安全信息

• 海关编码：
  2924199090
• 危险性防范说明：
  P261,P264,P271,P280,P302+P352,P304+P340,P305+P351+P338,P312,P313,P337+P313,P362,P403+P233,P405,P501
• 危险性描述：
  H315,H319,H335

反应信息

• 作为反应物：
  描述：

  6-[6-(6-氨基己酰氨基)己酰氨基]己酸 在 sodium hydroxide 、 乙醇 、 氯仿 、 镍 、 苯甲醇 作用下， 生成 [6]6-amino-lin-penta[1=>6]hexanoylamino-hexanoic acid
  参考文献：
  名称：

  West, Faserforschung und Textiltechnik, 1954, vol. 5, p. 145,154

  摘要：

  DOI：
• 作为产物：
  描述：

  N-<6-(6-Benzyloxycarbonylamino-hexanoyl)-amino-hexanoyl>-6-amino-capronsaeure 在 氢溴酸 、 溶剂黄146 作用下， 生成 6-[6-(6-氨基己酰氨基)己酰氨基]己酸
  参考文献：
  名称：

  Rothe; Kunitz, Justus Liebigs Annalen der Chemie, 1957, vol. 609, p. 88,100

  摘要：

  DOI：

文献信息

• Rothe; Kunitz, Justus Liebigs Annalen der Chemie, 1957, vol. 609, p. 88,100
  作者：Rothe、Kunitz

  DOI：——

  日期：——
• Zahn; Determann, Chemische Berichte, 1957, vol. 90, p. 2176,2180
  作者：Zahn、Determann

  DOI：——

  日期：——
• West, Faserforschung und Textiltechnik, 1954, vol. 5, p. 145,153
  作者：West

  DOI：——

  日期：——
• West, Faserforschung und Textiltechnik, 1954, vol. 5, p. 145,151
  作者：West

  DOI：——

  日期：——
• Enzymatic synthesis of nylon-6 units in organic solvents containing low concentrations of water
  作者：Yasuyuki Kawashima、Kengo Yasuhira、Naoki Shibata、Yusuke Matsuura、Yusuke Tanaka、Masaaki Taniguchi、Yoshiaki Miyoshi、Masahiro Takeo、Dai-ichiro Kato、Yoshiki Higuchi、Seiji Negoro

  DOI：10.1016/j.molcatb.2010.02.006

  日期：2010.6

  NyIB' carboxylesterase, which is 88% homologous to functional 6-aminohexanoate-dimer hydrolase (NyIB) from Arthrobacter sp., possesses trace synthetic activity [0.0004 mu mol min(-1) mg(-1) (U/mg)] from 6-aminohexanoate (Ahx) to its oligomers in 90% tert-butyl alcohol. The synthetic activity and the ratio of the synthetic activity to the hydrolytic activity were significantly affected by amino acid substitutions at positions 181, 266 and 370. The synthetic activity was enhanced to 2.7 U/mg by G181D-H266N substitutions, and the activity was further enhanced in the G181D-H266N-D370Y triple mutant to a level approximately 10(4)-fold greater than the parental carboxylesterase form (3.4 U/mg), which was nearly equal to the ordinary hydrolytic activity in water (type A-mutants). Type A-mutants possessed more than 50% of the 6-aminohexanoate-linear dimer (Ald)-hydrolytic activity at 0-70% tert-butyl alcohol, but the synthetic reaction became predominant at 85-90% tert-butyl alcohol. In contrast, type B-mutants (G181E-H266N and G181N-H266N) possessed quite low levels of Aid-hydrolytic activity (<0.01 U/mg) at 0-70% tert-butyl alcohol. However, both the hydrolytic and synthetic activities were enhanced at higher concentrations, and the maximum activity was obtained at 90% tert-butyl alcohol for both hydrolysis and synthesis. In a type C-mutant (R187S-F264C-D370Y), the Ald-hydrolytic activity was enhanced to approximately 80-fold that of the parental carboxylesterase, but the mutant barely demonstrated any synthetic activity. On the basis of the three-dimensional structure of the Ald-bound enzyme and a kinetic study for typical mutant enzymes, we propose that the efficient enzymatic syntheses of nylon-6 units were achieved by (i) stable binding of the 1st-Ahx at the N-terminal region with Asp181, (ii) interaction of the 2nd-Ahx at the C-terminal region with Tyr370, and (iii) motion of Tyr170 that generated a closed form in the catalytic center of Ald hydrolase. (C) 2010 Elsevier B.V. All rights reserved.