tert-butyl N-[2-[2-[2-[[2-hydroxy-2-(4-hydroxyphenyl)acetyl]amino]ethoxy]ethoxy]ethyl]carbamate | 182227-44-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: tert-butyl N-[2-[2-[2-[[2-hydroxy-2-(4-hydroxyphenyl)acetyl]amino]ethoxy]ethoxy]ethyl]carbamate
• CAS: 182227-44-7
• 化学式: C₁₉H₃₀N₂O₇
• 分子量: 398.456
• InChiKey: YYQSSQWEISUNIU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.6
• 重原子数：
  28
• 可旋转键数：
  13
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  126
• 氢给体数：
  4
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  tert-butyl N-[2-[2-[2-[[2-hydroxy-2-(4-hydroxyphenyl)acetyl]amino]ethoxy]ethoxy]ethyl]carbamate 在 4,4'-二氨基二苯乙烯-2,2'-二磺酸 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 50.0h， 生成 N-[2-[2-(2-aminoethoxy)ethoxy]ethyl]-2-[4-[diethoxy(oxido)phosphaniumyl]oxyphenyl]-2-fluoroacetamide
  参考文献：
  名称：

  Activity-based fluorescent probes that target phosphatases

  摘要：

  We have successfully designed and synthesized two fluorescently-labeled, activity-based probes, Probe I and Probe 2, which were shown to label protein tyrosine phosphatases specifically, as well as other types of phosphatases. The probes were not reactive towards the other non-phosphatase enzymes tested. These probes may find potential applications in large-scale proteomic experiments whereby subclasses of proteins may be selectively identified. (C) 2003 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0040-4039(03)00348-4
• 作为产物：
  描述：

  1,8-二氨基-3,6-二氧杂辛烷 在 4-(dicyanomethylene)-2-methyl-6-(p-dimethylaminostyryl)-4H-pyran 、 1-羟基苯并三唑 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 30.0h， 生成 tert-butyl N-[2-[2-[2-[[2-hydroxy-2-(4-hydroxyphenyl)acetyl]amino]ethoxy]ethoxy]ethyl]carbamate
  参考文献：
  名称：

  A versatile mechanism based reaction probe for the direct selection of biocatalysts

  摘要：

  A mechanism based reaction probe was synthesized and shown to modify a bacterial phosphotriesterase; this strategy for generating a probe is general and should allow the isolation of a host of unique catalysts. Copyright (C) 1996 Elsevier Science Ltd

  DOI：

  10.1016/0960-894x(96)00379-4

文献信息

• Evaluation of sulfatase-directed quinone methide traps for proteomics
  作者：Janina Lenger、Marius Schröder、Eva C. Ennemann、Benjamin Müller、Chi-Huey Wong、Thomas Noll、Thomas Dierks、Sarah R. Hanson、Norbert Sewald

  DOI：10.1016/j.bmc.2011.04.044

  日期：2012.1

  through a unique catalytic aldehyde, which is introduced by a posttranslational oxidation. To profile active sulfatases in health and disease, activity-based proteomic tools are needed. Herein, quinone methide (QM) traps directed against sulfatases are evaluated as activity-based proteomic probes (ABPPs). Starting from a p-fluoromethylphenyl sulfate scaffold, enzymatically generated QM-traps can inactivate

  硫酸酯酶通过翻译后氧化引入的独特催化醛水解裂解硫酸酯。为了分析健康和疾病中的活性硫酸酯酶，需要基于活性的蛋白质组学工具。在此，针对硫酸酯酶的醌甲基化物 (QM) 陷阱被评估为基于活性的蛋白质组学探针 (ABPP)。从对氟甲基苯基硫酸盐支架开始，酶促产生的 QM 陷阱可以灭活来自铜绿假单胞菌和肺炎克雷伯菌的细菌芳基硫酸酯酶和人类类固醇硫酸酯酶。然而，多种酶产生的 QM 形成、扩散和非特异性标记纯化的酶。在复杂的蛋白质组中，QM 标记是硫酸酯酶依赖性的，但也是非特异性的。因此，氟甲基苯基硫酸盐是硫酸酯酶的不良 ABPP。
• A versatile mechanism based reaction probe for the direct selection of biocatalysts
  作者：Lee -Chiang Lo、Chih-Hung L. Lo、Kim D. Janda、Daniel B. Kassel、Frank M. Raushel

  DOI：10.1016/0960-894x(96)00379-4

  日期：1996.9

  A mechanism based reaction probe was synthesized and shown to modify a bacterial phosphotriesterase; this strategy for generating a probe is general and should allow the isolation of a host of unique catalysts. Copyright (C) 1996 Elsevier Science Ltd
• Activity-based fluorescent probes that target phosphatases
  作者：Qing Zhu、Xuan Huang、Grace Y.J. Chen、Shao Q. Yao

  DOI：10.1016/s0040-4039(03)00348-4

  日期：2003.3

  We have successfully designed and synthesized two fluorescently-labeled, activity-based probes, Probe I and Probe 2, which were shown to label protein tyrosine phosphatases specifically, as well as other types of phosphatases. The probes were not reactive towards the other non-phosphatase enzymes tested. These probes may find potential applications in large-scale proteomic experiments whereby subclasses of proteins may be selectively identified. (C) 2003 Elsevier Science Ltd. All rights reserved.