benzotriazol-1-yl anthranilate | 88744-37-0

• 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: benzotriazol-1-yl anthranilate
• 英文别名: Benzotriazol-1-yl 2-aminobenzoate
• CAS: 88744-37-0
• 化学式: C₁₃H₁₀N₄O₂
• 分子量: 254.248
• InChiKey: JPKNQONFNZKKLX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  19
• 可旋转键数：
  3
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  83
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  benzotriazol-1-yl anthranilate 在 三乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 0.17h， 生成 Z-Gly-Ant-Gly-OTmb
  参考文献：
  名称：

  Stewart, Frederick H. C., Australian Journal of Chemistry, 1983, vol. 36, # 8, p. 1629 - 1638

  摘要：

  DOI：
• 作为产物：
  描述：

  1-羟基苯并三唑 、 邻氨基苯甲酸 在 吡啶 、 N,N'-二环己基碳二亚胺 作用下， 以 1,4-二氧六环 为溶剂， 以90%的产率得到benzotriazol-1-yl anthranilate
  参考文献：
  名称：

  Stewart, Frederick H. C., Australian Journal of Chemistry, 1983, vol. 36, # 8, p. 1629 - 1638

  摘要：

  DOI：

文献信息

• Chemoenzymatic synthesis of new fluorogenous substrates for cysteine proteases of the papain family
  作者：T. A. Semashko、E. N. Lysogorskaya、E. S. Oksenoit、A. V. Bacheva、I. Yu. Filippova

  DOI：10.1134/s1068162008030151

  日期：2008.5

  A chemoenzymatic synthesis was developed for new highly specific fluorogenic substrates for cysteine proteases of the papain family, Abz-Phe-Ala-pNA (I) and Glp-Phe-Ala-Amc (II) (Abz, pNA, Glp, and Amc are o-aminobenzoyl,p-nitroanilide, pyroglutamyl, and 4-amino-7-methylcoumaride, respectively). Substrate (I) was obtained in an aqueous-organic medium using native chymotrypsin. Substrate (II) was synthesized in DMF-MeCN by the treatment with chymotrypsin and subtilisin Carlsberg immobilized on polyvinyl alcohol cryogel. Hydrolysis of substrate (I) with papain, ficin, and bromelain was accompanied by a 15-fold increase in fluorescence intensity, and that of substrate (II), by a change in the fluorescence spectrum. Unambiguity of enzymatic hydrolysis of the substrates after the Ala residue was shown. The specific activity of the substrate hydrolysis with papain, bromelain, and ficin and was determined. Papain showed the greatest activity for both substrates. The activity of all proteases under study was essentially higher for substrate (II), than for substrate (I). The lowest detectable papain concentrations were 2.4 x 10(-10) M for (I) and 1.2 x 10(-11) M for (II). A high selectivity of cysteine proteases for Glp-Phe-Ala-Ame was established.
• Stewart, Frederick H. C., Australian Journal of Chemistry, 1983, vol. 36, # 8, p. 1629 - 1638
  作者：Stewart, Frederick H. C.

  DOI：——

  日期：——