(-)-indolactam I | 132738-83-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吲哚及其衍生物
• 英文名称: (-)-indolactam I
• 英文别名: (10S,13S)-10-[(2S)-butan-2-yl]-13-(hydroxymethyl)-9-methyl-3,9,12-triazatricyclo[6.6.1.04,15]pentadeca-1,4(15),5,7-tetraen-11-one
• CAS: 132738-83-1
• 化学式: C₁₈H₂₅N₃O₂
• 分子量: 315.415
• InChiKey: YPGSBXVZUVIXTK-BNLOLNQZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  23
• 可旋转键数：
  3
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  68.4
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  N-叔丁氧羰基-N-甲基-L-异亮氨酸 以 水 为溶剂， 反应 48.0h， 生成 (-)-indolactam I
  参考文献：
  名称：

  吲哚生物碱肿瘤启动子teleocidins的新同源物（-）-吲哚内酰胺I的分离和生物合成

  摘要：

  从稻瘟病链霉菌中分离出吲哚生物碱肿瘤启动子teleoocidins的新同源物（-）-吲哚内酰胺I，并显示其是由N-甲基-L-异亮氨酰-L-色氨酸进行生物合成的。

  DOI：

  10.1016/s0040-4039(00)88559-7

文献信息

• Synthesis of new indolactam analogues by microbial conversion
  作者：Shin-ichiro Kajiyama、Kazuhiro lrie、Takae Kido、Koichi Koshimizu、Hideo Hayashi、Motoo Arai

  DOI：10.1016/s0040-4020(01)80978-9

  日期：1991.7

  Abu, γ,δ-Δ-Nva, Nva, Nle, tert-Leu, Leu, Ile, allo-Ile. Phg instead ofL-Val in (−)-indolactam-Val, were synthesized from their seco-compounds (N-methyl-L-amino acidyl-L-tryptophonol) by microbial conversion.

  与L-Ala，Abu，γ，δ-Δ-Nva，Nva，Nle，ter-Leu，Leu，Ile，allo-Ile的十个吲哚内酰胺同类物。通过微生物转化，由它们的山高化合物（N-甲基-L-氨基酸基-L-色酚）合成了Phg而不是（-）-吲哚内酰胺-Val中的L-Val。
• The total synthesis of (−)-indolactam I
  作者：Manuel Mendoza、Niveda Rao、UyenPhuong Tran、Catherine Castaneda、Kelvin L. Billingsley

  DOI：10.1016/j.tet.2019.04.069

  日期：2019.8

  The first total synthesis of (−)-indolactam I (1) is reported. An efficient synthetic route was established to furnish the natural product in 8 steps. This strategy employed a copper-catalyzed amino acid arylation, peptide coupling, and Lewis acid-mediated macrocyclization to yield 1 from readily available building blocks. In addition, the cell growth inhibition activity of the natural product was

  报告了（-）-吲哚内酰胺I（1）的第一个全合成。建立了一种有效的合成途径来分8步提供天然产物。该策略采用了铜催化的氨基酸芳基化，肽偶联和路易斯酸介导的大环化，从易于获得的结构单元中获得1。另外，通过用K562白血病细胞系的测定来检查天然产物的细胞生长抑制活性。
• Enzymatic Production of (−)-Indolactam V by LtxB, a Cytochrome P450 Monooxygenase
  作者：Minh U. Huynh、Matthew C. Elston、Nick M. Hernandez、David B. Ball、Shin-ichiro Kajiyama、Kazuhiro Irie、William H. Gerwick、Daniel J. Edwards

  DOI：10.1021/np900481a

  日期：2010.1.22

  The P450 cytochrome monooxygenase gene, ltxB, was cloned and overexpressed in Escherichia coli as a 6xHis-taoged protein. The resulting recombinant LtxB was purified by Ni-NTA affinity chromatography and characterized biochemically. Purified LtxB demonstrated typical cytochrome P450 spectroscopic properties including substrate-induced transition from a low-spin (lambda(max) = 414 nm) to high-spin state (lambda(max) = 386 nm) upon incubation with N-methyl-L-valyl-L-tryptophanol. The catalytic activity of LtxB was verified by demonstrating the oxidation/cyclization of N-methyl-L-valyl-L-tryptophanol to (-)-indolactam V. LtxB shows a relaxed specificity for analogue substrates in which the valyl group is substituted for other aliphatic groups. The relaxed substrate specificity of LtxB, along with the relaxed specificity of the prenyltransferase, LtxC, allowed for the enzymatic production of a series of (-)-indolactam V and lyngbyatoxin analogues.