Suc-AAPD-pNA | 165174-58-3

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: Suc-AAPD-pNA
• 英文别名: Suc-Ala-Ala-Pro-Asp-pNA；(3S)-3-[[(2S)-1-[(2S)-2-[[(2S)-2-(3-carboxypropanoylamino)propanoyl]amino]propanoyl]pyrrolidine-2-carbonyl]amino]-4-(4-nitroanilino)-4-oxobutanoic acid
• CAS: 165174-58-3
• 化学式: C₂₅H₃₂N₆O₁₁
• 分子量: 592.563
• InChiKey: MBLUIJQGADPFTG-USJZOSNVSA-N

物化性质

• 沸点：
  1102.8±65.0 °C(Predicted)
• 密度：
  1.453±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -1.7
• 重原子数：
  42
• 可旋转键数：
  13
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.48
• 拓扑面积：
  257
• 氢给体数：
  6
• 氢受体数：
  11

反应信息

• 作为反应物：
  描述：

  Suc-AAPD-pNA 在 Streptomyces griseus protease B 作用下， 以 二甲基亚砜 为溶剂， 生成 4-硝基苯胺
  参考文献：
  名称：

  Cleavage of peptide bonds bearing ionizable amino acids at P1 by serine proteases with hydrophobic S1 pocket

  摘要：

  Enzymatic hydrolysis of the synthetic substrate succinyl-Ala-Ala-Pro-Xxx-pNA (where Xxx = Leu, Asp or Lys) catalyzed by bovine chymotrypsin (CHYM) or Streptomyces griseus protease B (SGPB) has been studied at different pH values in the pH range 3-11. The pH optima for substrates having Leu, Asp, and Lys have been found to be 7.5-8.0, 5.5-6.0, and similar to 10, respectively. At the normally reported pH optimum (pH 7-8) of CHYM and SGPB, the substrate with Leu at the reactive site is more than 25,000-fold more reactive than that with Asp. However, when fully protonated, Asp is nearly as good a substrate as Leu. The pK values of the side chains of Asp and Lys in the hydrophobic SI pocket of CHYM and SGPB have been calculated from pH-dependent hydrolysis data and have been found to be about 9 for Asp and 7.4 and 9.7 for Lys for CHYM and SGPB, respectively. The results presented in this communication suggest a possible application of CHYM like enzymes in cleaving peptide bonds contributed by acidic amino acids between pH 5 and 6. (C) 2010 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.bbrc.2010.08.078