N-(2-bromo-acetoxy)succinimide

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡咯烷类
• 英文名称: N-(2-bromo-acetoxy)succinimide
• 英文别名: N-succinimidylbromoacetate；1-(2-Bromoacetyl)pyrrolidine-2,5-dione
• 化学式: C₆H₆BrNO₃
• 分子量: 220.023
• InChiKey: ODZCFWBINWBUAU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.3
• 重原子数：
  11
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  54.4
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  α-D-galactosamine 1-phosphate 、 N-(2-bromo-acetoxy)succinimide 在 氢氧化钾 作用下， 以 四氢呋喃 、 水 为溶剂， 以82%的产率得到2-(2-bromoacetamido)-2-deoxy-α-D-galactopyranosyl phosphate
  参考文献：
  名称：

  Syntheses of unnatural N-substituted UDP-galactosamines as alternative substrates for N-acetylgalactosaminyl transferases

  摘要：

  UDP-GalNAc analogues with slight modifications in the 2-acetamido group of the GalNAc moiety are prepared in order to study their role in the mechanism of the N-acetylgalactosaminyl transferase mediated glycosylation step. The analogues with N-propionyl, N-butyryl- and N-bromoacetyl-groups were synthesized, utilizing Khorana's morpholidate coupling method starting from D-galactosaminyl-l-phosphate after selective N-acylation of its amino group with the appropriate N-acyloxysuccinimides. Furthermore. in addition to UDP-galactosamine its 2-azido analogue has been efficiently prepared involving a metal catalyzed diazo transfer reaction. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0008-6215(02)00183-0

文献信息

• Reduction of an Aldehyde by a NADH/Zn²⁺-Dependent Redox Active Ribozyme
  作者：Shinya Tsukiji、Swetansu B. Pattnaik、Hiroaki Suga

  DOI：10.1021/ja0495213

  日期：2004.4.28

  We report here the ability of an alcohol dehydrogenase (ADH) ribozyme to reduce a benzaldehyde. While the ribozyme was initially evolved in vitro based on the activity for the NAD+-dependent oxidation of the benzyl alcohol, we found that this ADH ribozyme is also capable of reducing the aldehyde in the presence of NADH and Zn2+. The rate acceleration gained by ribozyme catalysis was more than 6 orders of magnitude larger than the spontaneous reaction. Although the reversibility of phosphordiester and acyl transfer reactions catalyzed by ribozymes was known, that of other chemical reactions has not been well established. This study has demonstrated the reversibility of a hydride transfer chemistry catalyzed by the ADH ribozyme. Most interestingly, the ribozyme shares many features with the protein ADHs, e.g., reversibility and NADH/Zn2+ dependence.
• Syntheses of unnatural N-substituted UDP-galactosamines as alternative substrates for N-acetylgalactosaminyl transferases
  作者：Daniel Lazarevic、Joachim Thiem

  DOI：10.1016/s0008-6215(02)00183-0

  日期：2002.11

  UDP-GalNAc analogues with slight modifications in the 2-acetamido group of the GalNAc moiety are prepared in order to study their role in the mechanism of the N-acetylgalactosaminyl transferase mediated glycosylation step. The analogues with N-propionyl, N-butyryl- and N-bromoacetyl-groups were synthesized, utilizing Khorana's morpholidate coupling method starting from D-galactosaminyl-l-phosphate after selective N-acylation of its amino group with the appropriate N-acyloxysuccinimides. Furthermore. in addition to UDP-galactosamine its 2-azido analogue has been efficiently prepared involving a metal catalyzed diazo transfer reaction. (C) 2002 Elsevier Science Ltd. All rights reserved.