sodium p-nitrophenyl hydrogen phosphate | 4154-43-2

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机磷酸及其衍生物
• 英文名称: sodium p-nitrophenyl hydrogen phosphate
• 英文别名: sodium p-nitrophenyl phosphate；sodium;(4-nitrophenyl) hydrogen phosphate
• CAS: 4154-43-2
• 化学式: C₆H₅NO₆P*Na
• 分子量: 241.072
• InChiKey: RUYANEADGUFWRJ-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -2.56
• 重原子数：
  15
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  115
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  sodium p-nitrophenyl hydrogen phosphate 在 vaccinia H₁-related protein member Z 、 1,4-二巯基-2,3-丁二醇 作用下， 生成 对硝基苯酚
  参考文献：
  名称：

  New Functional Aspects of the Atypical Protein Tyrosine Phosphatase VHZ

  摘要：

  LDP3 (VHZ) is the smallest classical protein tyrosine phosphatase (PTP) known to date and was originally misclassified as an atypical dual-specificity phosphatase. Kinetic isotope effects with steady-state and pre-steady-state kinetics of VHZ and mutants with p-nitrophenol phosphate have revealed several unusual properties. VHZ is significantly more active than previously reported but remains one of the least active PTPs. Highly unusual for a PTP, VHZ possesses two acidic residues (E134 and D65) in the active site. D65 occupies the position corresponding to the typical general acid in the PTP family. However, VHZ primarily utilizes E134 as the general acid, with D65 taking over this role when E134 is mutated. This unusual behavior is facilitated by two coexisting, but unequally populated, substrate binding modes. Unlike most classical PTPs, VHZ exhibits phosphotransferase activity. Despite the presence of the Q-loop that normally prevents alcoholysis of the phosphoenzyme intermediate in other classical PTPs, VHZ readily phosphorylates ethylene glycol. Although mutations of Q-loop residues affect this phosphotransferase activity, mutations on the IPD loop that contains the general acid exert more control over this process. A single P68V substitution on this loop completely abolishes phosphotransferase activity. The ability of native VHZ to catalyze transphosphorylation may lead to an imbalance of intracellular phosphorylation, which could explain the correlation of its overexpression with several types of cancer.

  DOI：

  10.1021/bi400776z
• 作为产物：
  描述：

  sodium bis(4-nitrophenyl) phosphate 在 phosphodiesterase immobilized on amine-glutaraldehyde-functionalized-3-aminopropyltriethoxysilane-coated borosilicate reactor tube 作用下， 以 aq. buffer 为溶剂， 生成 对硝基苯酚 、 sodium p-nitrophenyl hydrogen phosphate
  参考文献：
  名称：

  Rapid protein immobilization for thin film continuous flow biocatalysis

  摘要：

  连续流生物催化学有了新的突破。为涡旋流体处理开发了一种高效且通用的酶固定化技术。固定化酶在连续流中表现出10小时内没有酶活性下降，并且所需试剂和酶的数量减少了95%以上。

  DOI：

  10.1039/c6cc04210d

文献信息

• Mechanism of phosphodiester cleavage with .beta.-cyclodextrin
  作者：Alvan C. Hengge、W. W. Cleland

  DOI：10.1021/jo00005a064

  日期：1991.3
• Functional group convergency in a binuclear dephosphorylation reagent
  作者：David H. Vance、Anthony W. Czarnik

  DOI：10.1021/ja00078a065

  日期：1993.12
• Rapid protein immobilization for thin film continuous flow biocatalysis
  作者：Joshua Britton、Colin L. Raston、Gregory A. Weiss

  DOI：10.1039/c6cc04210d

  日期：——

  Continuous flow biocatalysis gets a new spin. An efficient and general enzyme immobilization technique for vortex fluidic processing has been developed. The immobilized enzyme demonstrated no decrease in enzyme activity over 10 h in continuous flow with a >95% reduction in quantities of required reagents and enzymes.

  连续流生物催化学有了新的突破。为涡旋流体处理开发了一种高效且通用的酶固定化技术。固定化酶在连续流中表现出10小时内没有酶活性下降，并且所需试剂和酶的数量减少了95%以上。
• New Functional Aspects of the Atypical Protein Tyrosine Phosphatase VHZ
  作者：Vyacheslav I. Kuznetsov、Alvan C. Hengge

  DOI：10.1021/bi400776z

  日期：2013.11.12

  LDP3 (VHZ) is the smallest classical protein tyrosine phosphatase (PTP) known to date and was originally misclassified as an atypical dual-specificity phosphatase. Kinetic isotope effects with steady-state and pre-steady-state kinetics of VHZ and mutants with p-nitrophenol phosphate have revealed several unusual properties. VHZ is significantly more active than previously reported but remains one of the least active PTPs. Highly unusual for a PTP, VHZ possesses two acidic residues (E134 and D65) in the active site. D65 occupies the position corresponding to the typical general acid in the PTP family. However, VHZ primarily utilizes E134 as the general acid, with D65 taking over this role when E134 is mutated. This unusual behavior is facilitated by two coexisting, but unequally populated, substrate binding modes. Unlike most classical PTPs, VHZ exhibits phosphotransferase activity. Despite the presence of the Q-loop that normally prevents alcoholysis of the phosphoenzyme intermediate in other classical PTPs, VHZ readily phosphorylates ethylene glycol. Although mutations of Q-loop residues affect this phosphotransferase activity, mutations on the IPD loop that contains the general acid exert more control over this process. A single P68V substitution on this loop completely abolishes phosphotransferase activity. The ability of native VHZ to catalyze transphosphorylation may lead to an imbalance of intracellular phosphorylation, which could explain the correlation of its overexpression with several types of cancer.