6-(Ethoxyoxalyl-amino)-1-methyl-1H-indole-5-carboxylic acid ethyl ester | 849468-08-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡咯并吡啶类
• 英文名称: 6-(Ethoxyoxalyl-amino)-1-methyl-1H-indole-5-carboxylic acid ethyl ester
• CAS: 849468-08-2
• 化学式: C₁₆H₁₈N₂O₅
• 分子量: 318.329
• InChiKey: OBLCCECPCCMOTE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.86
• 重原子数：
  23.0
• 可旋转键数：
  4.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  86.63
• 氢给体数：
  1.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  6-(Ethoxyoxalyl-amino)-1-methyl-1H-indole-5-carboxylic acid ethyl ester 在 sodium hydroxide 作用下， 以 乙醇 为溶剂， 反应 16.0h， 生成 1-methyl-6-(oxalylamino)indole-5-carboxylic acid
  参考文献：
  名称：

  Allele-Specific Inhibitors of Protein Tyrosine Phosphatases

  摘要：

  Protein tyrosine phosphatases (PTPs) are critical cell-signaling molecules. Inhibitors that are selective for individual PTPs would be valuable tools for dissecting complicated phosphorylation networks. However, the common architecture of PTP active sites impedes the discovery of such compounds. To achieve target selectivity, we have redesigned a PTP/inhibitor interface. Site-directed mutagenesis of a prototypical phosphatase, PTP1B, was used to generate "inhibitor-sensitized" PTPs. The PTP1B mutants were targeted by modifying a broad specificity PTP inhibitor with chemical groups that are sterically incompatible with wild-type PTP active sites. From a small panel of putative inhibitors, compounds that selectively inhibit Ile219Ala PTP1B over the wild-type enzyme were identified. Importantly, the corresponding mutation also conferred novel inhibitor sensitivity to T-cell PTP, suggesting that a readily identifiable point mutation can be used to generate a variety of inhibitor-sensitive PTPs.

  DOI：

  10.1021/ja043378w
• 作为产物：
  描述：

  草酰氯单乙酯 、 6-Amino-1-methyl-1H-indole-5-carboxylic acid ethyl ester 以 四氢呋喃 为溶剂， 生成 6-(Ethoxyoxalyl-amino)-1-methyl-1H-indole-5-carboxylic acid ethyl ester
  参考文献：
  名称：

  Allele-Specific Inhibitors of Protein Tyrosine Phosphatases

  摘要：

  Protein tyrosine phosphatases (PTPs) are critical cell-signaling molecules. Inhibitors that are selective for individual PTPs would be valuable tools for dissecting complicated phosphorylation networks. However, the common architecture of PTP active sites impedes the discovery of such compounds. To achieve target selectivity, we have redesigned a PTP/inhibitor interface. Site-directed mutagenesis of a prototypical phosphatase, PTP1B, was used to generate "inhibitor-sensitized" PTPs. The PTP1B mutants were targeted by modifying a broad specificity PTP inhibitor with chemical groups that are sterically incompatible with wild-type PTP active sites. From a small panel of putative inhibitors, compounds that selectively inhibit Ile219Ala PTP1B over the wild-type enzyme were identified. Importantly, the corresponding mutation also conferred novel inhibitor sensitivity to T-cell PTP, suggesting that a readily identifiable point mutation can be used to generate a variety of inhibitor-sensitive PTPs.

  DOI：

  10.1021/ja043378w