(6S,9S,12S,E)-methyl 9-(4-((tert-butoxycarbonyl)amino)butyl)-6,12-diisopropyl-2,2-dimethyl-4,7,10-trioxo-3-oxa-5,8,11-triazapentadec-13-en-15-oate | 1326714-37-7

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (6S,9S,12S,E)-methyl 9-(4-((tert-butoxycarbonyl)amino)butyl)-6,12-diisopropyl-2,2-dimethyl-4,7,10-trioxo-3-oxa-5,8,11-triazapentadec-13-en-15-oate
• CAS: 1326714-37-7
• 化学式: C₂₉H₅₂N₄O₈
• 分子量: 584.754
• InChiKey: BZCZKQRYLLYUPO-KMQHNPFOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.59
• 重原子数：
  41.0
• 可旋转键数：
  14.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.76
• 拓扑面积：
  161.16
• 氢给体数：
  4.0
• 氢受体数：
  8.0

反应信息

• 作为反应物：
  描述：

  (6S,9S,12S,E)-methyl 9-(4-((tert-butoxycarbonyl)amino)butyl)-6,12-diisopropyl-2,2-dimethyl-4,7,10-trioxo-3-oxa-5,8,11-triazapentadec-13-en-15-oate 在 potassium hydrogencarbonate 、 三乙胺 、 lithium hydroxide 作用下， 以 四氢呋喃 、 甲醇 、 水 为溶剂， 反应 12.5h， 生成 (6S,9S,12S,E)-9-(4-((tert-butoxycarbonyl)amino)butyl)-6,12-diisopropyl-2,2-dimethyl-4,7,10-trioxo-3-oxa-5,8,11-triazapentadec-13-en-15-oic-CoA
  参考文献：
  名称：

  Enzymatic Timing and Tailoring of Macrolactamization in Syringolin Biosynthesis

  摘要：

  The enzymatic activation of 3,4-dehydrolysine and subsequent formation of the 12-membered syringolin macrolactam were investigated. The timing of the desaturation was elucidated through the analysis of the initial adenylation domain of SylD. The SylD-TTE didomain was characterized and demonstrated to be the catalyst for formation of 12-membered macrocycles. When the SylD thioesterase domain was reacted with a family of acyclic CoA both natural and unnatural macrocycles were generated.

  DOI：

  10.1021/ol2016687
• 作为产物：
  描述：

  (S,E)-methyl 4-amino-5-methylhex-2-enoate 在 哌啶 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 24.5h， 生成 (6S,9S,12S,E)-methyl 9-(4-((tert-butoxycarbonyl)amino)butyl)-6,12-diisopropyl-2,2-dimethyl-4,7,10-trioxo-3-oxa-5,8,11-triazapentadec-13-en-15-oate
  参考文献：
  名称：

  Enzymatic Timing and Tailoring of Macrolactamization in Syringolin Biosynthesis

  摘要：

  The enzymatic activation of 3,4-dehydrolysine and subsequent formation of the 12-membered syringolin macrolactam were investigated. The timing of the desaturation was elucidated through the analysis of the initial adenylation domain of SylD. The SylD-TTE didomain was characterized and demonstrated to be the catalyst for formation of 12-membered macrocycles. When the SylD thioesterase domain was reacted with a family of acyclic CoA both natural and unnatural macrocycles were generated.

  DOI：

  10.1021/ol2016687