anthraquinone-2-carbonyl-N-acetylcysteamine | 1198158-09-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 蒽
• 英文名称: anthraquinone-2-carbonyl-N-acetylcysteamine
• 英文别名: anthraquinone-2-carboxylic acid-NAC；anthraquinone-2-carboxyate-N-acetylcysteamine；S-(2-acetamidoethyl) 9,10-dioxoanthracene-2-carbothioate
• CAS: 1198158-09-6
• 化学式: C₁₉H₁₅NO₄S
• 分子量: 353.398
• InChiKey: HGRWURYRDUESSW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.6
• 重原子数：
  25
• 可旋转键数：
  5
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.16
• 拓扑面积：
  106
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  N-乙酰基半胱胺 、 蒽醌-2-羧酸 在 4-二甲氨基吡啶 、 聚碳化二亚胺 作用下， 以 二氯甲烷 为溶剂， 反应 16.0h， 以90%的产率得到anthraquinone-2-carbonyl-N-acetylcysteamine
  参考文献：
  名称：

  Physically Discrete β-Lactamase-Type Thioesterase Catalyzes Product Release in Atrochrysone Synthesis by Iterative Type I Polyketide Synthase

  摘要：

  ATEG_08451 in Aspergillus terreus, here named atrochrysone carboxylic acid synthase (ACAS), is a nonreducing, iterative type I polyketide synthase that contains no thioesterase domain. In vitro, reactions of ACAS with malonyl-CoA yielded a polyketide intermediate, probably attached to its acyl carrier protein (ACP). The addition of ATEG_08450, here named atrochrysone carboxyl ACP thioesterase (ACTE), to the reaction resulted in the release of products derived from atrochrysone carboxylic acid, such as atrochrysone and endocrocin. ACTE, belonging to the beta-lactamase superfamily, thus appears to be a novel type of thioesterase responsible for product release in polyketide biosynthesis. These findings show that ACAS synthesizes the scaffold of atrochrysone carboxylic acid from malonyl-CoA, and that ACTE hydrolyzes the thioester bond between the ACP of ACAS and the intermediate to release atrochrysone carboxylic acid as the reaction product.

  DOI：

  10.1016/j.chembiol.2009.04.004

文献信息

• Physically Discrete β-Lactamase-Type Thioesterase Catalyzes Product Release in Atrochrysone Synthesis by Iterative Type I Polyketide Synthase
  作者：Takayoshi Awakawa、Kosuke Yokota、Nobutaka Funa、Fuminao Doi、Naoki Mori、Hidenori Watanabe、Sueharu Horinouchi

  DOI：10.1016/j.chembiol.2009.04.004

  日期：2009.6

  ATEG_08451 in Aspergillus terreus, here named atrochrysone carboxylic acid synthase (ACAS), is a nonreducing, iterative type I polyketide synthase that contains no thioesterase domain. In vitro, reactions of ACAS with malonyl-CoA yielded a polyketide intermediate, probably attached to its acyl carrier protein (ACP). The addition of ATEG_08450, here named atrochrysone carboxyl ACP thioesterase (ACTE), to the reaction resulted in the release of products derived from atrochrysone carboxylic acid, such as atrochrysone and endocrocin. ACTE, belonging to the beta-lactamase superfamily, thus appears to be a novel type of thioesterase responsible for product release in polyketide biosynthesis. These findings show that ACAS synthesizes the scaffold of atrochrysone carboxylic acid from malonyl-CoA, and that ACTE hydrolyzes the thioester bond between the ACP of ACAS and the intermediate to release atrochrysone carboxylic acid as the reaction product.