5-[5-(2-oxohexahydrothieno[3,4-d]imidazol-6-yl)pentanoylamino]pentanoic acid | 443770-03-4

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 生物素及其衍生物
• 英文名称: 5-[5-(2-oxohexahydrothieno[3,4-d]imidazol-6-yl)pentanoylamino]pentanoic acid
• 英文别名: 5-(5-((3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamido)pentanoic acid；5-[5-[(3aS,4S,6aR)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]pentanoylamino]pentanoic acid
• CAS: 443770-03-4
• 化学式: C₁₅H₂₅N₃O₄S
• 分子量: 343.447
• InChiKey: BOPWGSSJXAVKLP-MJVIPROJSA-N

物化性质

• 沸点：
  722.5±55.0 °C(Predicted)
• 密度：
  1?+-.0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.3
• 重原子数：
  23
• 可旋转键数：
  10
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.8
• 拓扑面积：
  133
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  双[2-(二苯基膦基)乙基]胺盐酸盐 、 5-[5-(2-oxohexahydrothieno[3,4-d]imidazol-6-yl)pentanoylamino]pentanoic acid 在 N-甲基吗啉 、 2-氯-4,6-二甲氧基-1,3,5-三嗪 作用下， 以 乙腈 为溶剂， 以34%的产率得到5-(2-oxohexahydrothieno[3,4-d]imidazol-6-yl)pentanoic acid {4-[bis(2-diphenylphosphanyl-ethyl)carbamoyl]butyl}amide
  参考文献：
  名称：

  Artificial Metalloenzymes:  (Strept)avidin as Host for Enantioselective Hydrogenation by Achiral Biotinylated Rhodium−Diphosphine Complexes

  摘要：

  We report on the generation of artificial metalloenzymes based on the noncovalent incorporation of biotinylated rhodium-diphosphine complexes in (strept)avidin as host proteins. A chemogenetic optimization procedure allows one to optimize the enantioselectivity for the reduction of acetamidoacrylic acid (up to 96% ee (R) in streptavidin S112G and up to 80% ee (S) in WT avidin). The association constant between a prototypical cationic biotinylated rhodium-diphosphine catalyst precursor and the host proteins was determined at neutral pH: log K-a = 7.7 for avidin (pl = 10.4) and log K-a = 7.1 for streptavidin (pl = 6.4). It is shown that the optimal operating conditions for the enantioselective reduction are 5 bar at 30 degreesC with a 1% catalyst loading.

  DOI：

  10.1021/ja0476718
• 作为产物：
  描述：

  D-生物素 、 5-氨基颉草酸 在 三正丁胺 、 氯甲酸异丁酯 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 2.17h， 以73%的产率得到5-[5-(2-oxohexahydrothieno[3,4-d]imidazol-6-yl)pentanoylamino]pentanoic acid
  参考文献：
  名称：

  Artificial Metalloenzymes:  (Strept)avidin as Host for Enantioselective Hydrogenation by Achiral Biotinylated Rhodium−Diphosphine Complexes

  摘要：

  We report on the generation of artificial metalloenzymes based on the noncovalent incorporation of biotinylated rhodium-diphosphine complexes in (strept)avidin as host proteins. A chemogenetic optimization procedure allows one to optimize the enantioselectivity for the reduction of acetamidoacrylic acid (up to 96% ee (R) in streptavidin S112G and up to 80% ee (S) in WT avidin). The association constant between a prototypical cationic biotinylated rhodium-diphosphine catalyst precursor and the host proteins was determined at neutral pH: log K-a = 7.7 for avidin (pl = 10.4) and log K-a = 7.1 for streptavidin (pl = 6.4). It is shown that the optimal operating conditions for the enantioselective reduction are 5 bar at 30 degreesC with a 1% catalyst loading.

  DOI：

  10.1021/ja0476718

文献信息

• US7943595B2
  申请人：——

  公开号：US7943595B2

  公开（公告）日：2011-05-17
• Artificial Metalloenzymes:  (Strept)avidin as Host for Enantioselective Hydrogenation by Achiral Biotinylated Rhodium−Diphosphine Complexes
  作者：Myriem Skander、Nicolas Humbert、Jérôme Collot、Julieta Gradinaru、Gérard Klein、Andreas Loosli、Jérôme Sauser、Andrea Zocchi、François Gilardoni、Thomas R. Ward

  DOI：10.1021/ja0476718

  日期：2004.11.1

  We report on the generation of artificial metalloenzymes based on the noncovalent incorporation of biotinylated rhodium-diphosphine complexes in (strept)avidin as host proteins. A chemogenetic optimization procedure allows one to optimize the enantioselectivity for the reduction of acetamidoacrylic acid (up to 96% ee (R) in streptavidin S112G and up to 80% ee (S) in WT avidin). The association constant between a prototypical cationic biotinylated rhodium-diphosphine catalyst precursor and the host proteins was determined at neutral pH: log K-a = 7.7 for avidin (pl = 10.4) and log K-a = 7.1 for streptavidin (pl = 6.4). It is shown that the optimal operating conditions for the enantioselective reduction are 5 bar at 30 degreesC with a 1% catalyst loading.