p-nitrophenyl phosphate | 29314-29-2

• 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: p-nitrophenyl phosphate
• CAS: 29314-29-2
• 化学式: C₆H₅NO₆P
• 分子量: 218.083
• InChiKey: OUYBIBNVWITLBQ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  14.0
• 可旋转键数：
  3.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  106.74
• 氢给体数：
  1.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  p-nitrophenyl phosphate 在 acid phosphotase II from Aspergillus niger KU-8 、 水 作用下， 生成 对硝基苯酚
  参考文献：
  名称：

  Substrate Selectivity inAspergillus nigerKU-8 Acid Phosphatase II Using Phosphoryl Oligosaccharides

  摘要：

  The intracellular acid phosphatase II (ACPase II) produced by Aspergillus niger KU-8 preferentially dephosphorylates C-6 phosphate groups rather than C-3 phosphate groups of phosphoryl oligosaccharides. In this study, the kinetic parameters of ACPase II were measured. 32-phosphoryl maltotriose and 62-phosphoryl maltotriose, which differ only in the binding position of the phosphate group, were prepared and used as the substrates. The Km for both substrates were similar. However, the kcat value for the 62-phosphoryl maltotriose was about three-fold of that for the 32-phosphoryl maltotriose.

  DOI：

  10.1271/bbb.64.1534

文献信息

• Chukhrai, E. S.; Nikulina, V. S.; Poltorak, O. M., Russian Journal of Physical Chemistry, 1989, vol. 63, # 1, p. 141 - 143
  作者：Chukhrai, E. S.、Nikulina, V. S.、Poltorak, O. M.

  DOI：——

  日期：——
• Substrate Selectivity in<i>Aspergillus niger</i>KU-8 Acid Phosphatase II Using Phosphoryl Oligosaccharides
  作者：Kenji TO-O、Hiroshi KAMASAKA、Takashi KURIKI、Shigetaka OKADA

  DOI：10.1271/bbb.64.1534

  日期：2000.1

  The intracellular acid phosphatase II (ACPase II) produced by Aspergillus niger KU-8 preferentially dephosphorylates C-6 phosphate groups rather than C-3 phosphate groups of phosphoryl oligosaccharides. In this study, the kinetic parameters of ACPase II were measured. 32-phosphoryl maltotriose and 62-phosphoryl maltotriose, which differ only in the binding position of the phosphate group, were prepared and used as the substrates. The Km for both substrates were similar. However, the kcat value for the 62-phosphoryl maltotriose was about three-fold of that for the 32-phosphoryl maltotriose.