(S)-methyl 2-((S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-6-((tert-butoxycarbonyl)amino)hexanamido)-3-methylbutanoate | 1326714-29-7

• 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: (S)-methyl 2-((S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-6-((tert-butoxycarbonyl)amino)hexanamido)-3-methylbutanoate
• 英文别名: Fmoc-Lys(Boc)-Val-OMe；methyl (2S)-2-[[(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-6-[(2-methylpropan-2-yl)oxycarbonylamino]hexanoyl]amino]-3-methylbutanoate
• CAS: 1326714-29-7
• 化学式: C₃₂H₄₃N₃O₇
• 分子量: 581.709
• InChiKey: RCWXOWAUHTZKQF-SVBPBHIXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.5
• 重原子数：
  42
• 可旋转键数：
  16
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  132
• 氢给体数：
  3
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  (S)-methyl 2-((S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-6-((tert-butoxycarbonyl)amino)hexanamido)-3-methylbutanoate 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 、 lithium hydroxide 作用下， 以 甲醇 、 二氯甲烷 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 24.75h， 生成 (5S,9S,12S,15S)-12-(4-((tert-butoxycarbonyl)amino)butyl)-5,9,15-triisopropyl-2,2-dimethyl-4,7,10,13-tetraoxo-3-oxa-6,8,11,14-tetraazahexadecan-16-oic acid
  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：

  L-缬氨酸甲酯 、 N-alpha-芴甲氧羰基-N-epsilon-叔丁氧羰基-L-赖氨酸 在 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 为溶剂， 反应 12.0h， 以37%的产率得到(S)-methyl 2-((S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-6-((tert-butoxycarbonyl)amino)hexanamido)-3-methylbutanoate
  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