阿斯普尼辛 D | 93413-07-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 嘧啶二氮卓类
• 中文名称: 阿斯普尼辛 D
• 中文别名: 阿斯普尼辛D
• 英文名称: asperlicin D
• 英文别名: (7S)-7-(1H-indol-3-ylmethyl)-5,7-dihydroquinazolino[3,2-d][1,4]benzodiazepine-6,9-dione
• CAS: 93413-07-1
• 化学式: C₂₅H₁₈N₄O₂
• 分子量: 406.444
• InChiKey: TTYFXJZDLYVOTG-QFIPXVFZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.6
• 重原子数：
  31
• 可旋转键数：
  2
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.08
• 拓扑面积：
  77.6
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  L-色氨酸甲酯 在 三乙胺 、 magnesium chloride 作用下， 以 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 反应 36.0h， 生成 阿斯普尼辛 D
  参考文献：
  名称：

  Total synthesis of asperlicin D

  摘要：

  Cyclodehydration of a linear tripeptide furnished the first total synthesis of asperlicin D in moderate yield. The cyclodehydration process was triggered by an intramolecular nucleophilic acyl substitution and an intramolecular aza-Wittig reaction. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetlet.2005.11.123

文献信息

• An Iterative, Bimodular Nonribosomal Peptide Synthetase that Converts Anthranilate and Tryptophan into Tetracyclic Asperlicins
  作者：Xue Gao、Wei Jiang、Gonzalo Jiménez-Osés、Moon Seok Choi、Kendall N. Houk、Yi Tang、Christopher T. Walsh

  DOI：10.1016/j.chembiol.2013.04.019

  日期：2013.7

  anthranilate (Ant) into a pair of tetracyclic peptidyl alkaloids asperlicin C and D in a ratio of 10:1. The first module of AspA activates and processes two molecules of Ant iteratively to generate a tethered Ant-Ant-Trp-S-enzyme intermediate on module two. Release is postulated to involve tandem cyclizations, in which the first step is the macrocyclization of the linear tripeptidyl-S-enzyme, by the terminal

  来自葱曲霉的双模块 276 kDa 非核糖体肽合成酶 AspA，在酿酒酵母中异源表达，将色氨酸和两分子芳香族 β-氨基酸邻氨基苯甲酸 (Ant) 转化为一对四环肽基生物碱 D: asperlicin D: asperlicin . AspA 的第一个模块反复激活和处理两个 Ant 分子，以在模块 2 上生成一个连接的 Ant-Ant-Trp-S-酶中间体。假定释放涉及串联环化，其中第一步是线性三肽基-S-酶的大环化，通过末端缩合 (CT) 域生成区域异构四环 asperlicin 支架。
• Assembly of Asperlicin Peptidyl Alkaloids from Anthranilate and Tryptophan: A Two-Enzyme Pathway Generates Heptacyclic Scaffold Complexity in Asperlicin E
  作者：Stuart W. Haynes、Xue Gao、Yi Tang、Christopher T. Walsh

  DOI：10.1021/ja308371z

  日期：2012.10.24

  Members of the asperlicin family of fungal metabolites produced by Aspergillus alliaceus are known potent CCKA antagonists. Herein, we report the identification of the gene cluster responsible for directing their biosynthesis. We validate and probe the pathway by genetic manipulation, and provide the first biochemical characterization of the oxidative cyclization en route to the heptacyclic asperlicin E by reconstituting the activity of the FAD depend monooxygenase AspB. This report provides the first genetic characterization of a NRPS assembly line that efficiently activates two anthranilate building blocks and illustrates the remarkably efficient biosynthesis of the complex heptacyclic asperlicin E.