N-(6-nitroveratryloxycarbonyl)-L-threonine | 1236189-70-0

• 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: N-(6-nitroveratryloxycarbonyl)-L-threonine
• CAS: 1236189-70-0
• 化学式: C₁₄H₁₈N₂O₉
• 分子量: 358.305
• InChiKey: BGJMSLRDMDKDKX-KRTXAFLBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.67
• 重原子数：
  25.0
• 可旋转键数：
  8.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  157.46
• 氢给体数：
  3.0
• 氢受体数：
  8.0

反应信息

• 作为反应物：
  描述：

  N-(6-nitroveratryloxycarbonyl)-L-threonine 在 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 20.0h， 以65%的产率得到4,5-dimethoxy-2-nitrobenzyl ((2R,3S)-2-methyl-4-oxooxetan-3-yl)carbamate
  参考文献：
  名称：

  Synthesis of pdCpAs and transfer RNAs activated with thiothreonine and derivatives

  摘要：

  N,S-diprotected L-thiothreonine and L-allo-thiothreonine derivatives were synthesized using a novel chemical strategy, and used for esterification of the dinucleotide pdCpA. The aminoacylated dinucleotides were then employed for the preparation of activated suppressor tRNA(CUA) transcripts. Thiothreonine and allo-thiothreonine were incorporated into a predetermined position of a catalytically competent dihydrofolate reductase (DHFR) analogue lacking cysteine, and the elaborated proteins were derivatized site-specifically at the thiothreonine residue with a fluorophore. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2012.02.024
• 作为产物：
  描述：

  L-苏氨酸 、 4,5-二甲氧基-2-硝基苄基氯甲酸酯 在 碳酸氢钠 、 sodium hydrogen sulfate 作用下， 以 1,4-二氧六环 、 水 为溶剂， 反应 17.0h， 以85%的产率得到N-(6-nitroveratryloxycarbonyl)-L-threonine
  参考文献：
  名称：

  Synthesis of pdCpAs and transfer RNAs activated with thiothreonine and derivatives

  摘要：

  N,S-diprotected L-thiothreonine and L-allo-thiothreonine derivatives were synthesized using a novel chemical strategy, and used for esterification of the dinucleotide pdCpA. The aminoacylated dinucleotides were then employed for the preparation of activated suppressor tRNA(CUA) transcripts. Thiothreonine and allo-thiothreonine were incorporated into a predetermined position of a catalytically competent dihydrofolate reductase (DHFR) analogue lacking cysteine, and the elaborated proteins were derivatized site-specifically at the thiothreonine residue with a fluorophore. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2012.02.024