3-amino-5-[(1-oxopent-4-ynyl)amino]benzoic acid | 1092173-28-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 3-amino-5-[(1-oxopent-4-ynyl)amino]benzoic acid
• 英文别名: 3-Amino-5-(pent-4-ynoylamino)benzoic acid；3-amino-5-(pent-4-ynoylamino)benzoic acid
• CAS: 1092173-28-8
• 化学式: C₁₂H₁₂N₂O₃
• 分子量: 232.239
• InChiKey: WGXCRERMVLOCIU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.5
• 重原子数：
  17
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  92.4
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  4-戊炔酸琥珀亚胺酯 、 3,5-二氨基苯甲酸 在 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 以70%的产率得到3-amino-5-[(1-oxopent-4-ynyl)amino]benzoic acid
  参考文献：
  名称：

  Cu-free cycloaddition for identifying catalytic active adenylation domains of nonribosomal peptide synthetases by phage display

  摘要：

  To engineer the substrate specificities of nonribosomal peptide synthetases (NRPS), we developed a method to display NRPS modules on M13 phages and select catalytically active adenylation (A) domains that would load azide functionalized substrate analogs to the neighboring peptidyl carrier protein (PCP) domains. Biotin conjugated difluorinated cyclooctyne was used for copper free cycloaddition with an azide substituted substrate attached to PCP. Biotin-labeled phages were selected by binding to streptavidin. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2008.08.085

文献信息

• Cu-free cycloaddition for identifying catalytic active adenylation domains of nonribosomal peptide synthetases by phage display
  作者：Yekui Zou、Jun Yin

  DOI：10.1016/j.bmcl.2008.08.085

  日期：2008.10

  To engineer the substrate specificities of nonribosomal peptide synthetases (NRPS), we developed a method to display NRPS modules on M13 phages and select catalytically active adenylation (A) domains that would load azide functionalized substrate analogs to the neighboring peptidyl carrier protein (PCP) domains. Biotin conjugated difluorinated cyclooctyne was used for copper free cycloaddition with an azide substituted substrate attached to PCP. Biotin-labeled phages were selected by binding to streptavidin. (C) 2008 Elsevier Ltd. All rights reserved.