dicyclohexylammonium p-nitrophenyl phosphate | 58965-74-5

• 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: dicyclohexylammonium p-nitrophenyl phosphate
• 英文别名: N-cyclohexylcyclohexanamine;(4-nitrophenyl) dihydrogen phosphate
• CAS: 58965-74-5
• 化学式: C₆H₆NO₆P*C₁₂H₂₃N
• 分子量: 400.412
• InChiKey: LCUWBEOWXNIMKW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.31
• 重原子数：
  27
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  125
• 氢给体数：
  3
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  dicyclohexylammonium p-nitrophenyl phosphate 在 recombinant human protein-tyrosine phosphatase 1B 、 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：

  Insights into the Reaction of Protein-tyrosine Phosphatase 1B

  摘要：

  Catalysis by protein-tyrosine phosphatase 1B (PTP1B) occurs through a two-step mechanism involving a phosphocysteine intermediate. We have solved crystal structures for the transition state analogs for both steps. Together with previously reported crystal structures of apo-PTP1B, the Michaelis complex of an inactive mutant, the phosphoenzyme intermediate, and the product complex, a full picture of all catalytic steps can now be depicted. The transition state analog for the first catalytic step comprises a ternary complex between the catalytic cysteine of PTP1B, vanadate, and the peptide DADEYL, a fragment of a physiological substrate. The equatorial vanadate oxygen atoms bind to the P-loop, and the apical positions are occupied by the peptide tyrosine oxygen and by the PTP1B cysteine sulfur atom. The vanadate assumes a trigonal bipyramidal geometry in both transition state analog structures, with very similar apical O-O distances, denoting similar transition states for both phosphoryl transfer steps. Detailed interactions between the flanking peptide and the enzyme are discussed.

  DOI：

  10.1074/jbc.m109.066951
• 作为产物：
  描述：

  磷酸单硝基苯基酯 、 环己胺 在 sodium hydroxide 作用下， 以 氯仿 为溶剂， 生成 dicyclohexylammonium p-nitrophenyl phosphate
  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

文献信息

• Integral multilayer analytical element for use in the measurement of alkaline phosphatase acitivity
  申请人：FUJI PHOTO FILM CO., LTD.

  公开号：EP0182179A1

  公开（公告）日：1986-05-28

  An integral multilayer analytical element for use in the measurement of alkaline phosphatase activity, which comprises a porous spreading layer of woven fabric or knitted fabric containing an alkaline phosphatase-sensitive self-developing substrate, a buffer layer containing one or more compounds functioning as a phosphoric acid acceptor and a buffering agent and a support layer in a laminated form.

  一种用于测量碱性磷酸酶活性的整体式多层分析元件，它包括多孔的机织物或针织物铺展层，其中含有对碱性磷酸酶敏感的自显影基质；缓冲层，其中含有一种或多种用作磷酸受体和缓冲剂的化合物；以及层压形式的支撑层。
• Morrow, Janet R.; Richard, John P.; et al., Journal of the American Chemical Society, 2008, vol. 130, p. 17858 - 17866
  作者：Morrow, Janet R.、Richard, John P.、et al.、Humphry, Tim、Iyer, Subashree、Iranzo, Olga

  DOI：——

  日期：——
• The molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1B
  作者：Tiago A.S. Brandão、Sean J. Johnson、Alvan C. Hengge

  DOI：10.1016/j.abb.2012.06.002

  日期：2012.9

  The movement of a conserved protein loop (the WPD-loop) is important in catalysis by protein tyrosine phosphatases (PTPs). Using kinetics, isotope effects, and X-ray crystallography, the different effects arising from mutation of the conserved tryptophan in the WPD-loop were compared in two PTPs, the human PTP1B, and the bacterial YopH from Yersinia. Mutation of the conserved tryptophan in the WPD-loop to phenylalanine has a negligible effect on in PTP1B and full loop movement is maintained. In contrast, the corresponding mutation in YopH reduces k(cat) by two orders of magnitude and the WPD loop locks in an intermediate position, disabling general acid catalysis. During loop movement the indole moiety of the WPD-loop tryptophan moves in opposite directions in the two enzymes. Comparisons of mammalian and bacterial PTPs reveal differences in the residues forming the hydrophobic pocket surrounding the conserved tryptophan. Thus, although WPD-loop movement is a conserved feature in PTPs, differences exist in the molecular details, and in the tolerance to mutation, in PTP1B compared to YopH. Despite high structural similarity of the active sites in both WPD-loop open and closed conformations, differences are identified in the molecular details associated with loop movement in PTPs from different organisms. (C) 2012 Elsevier Inc. All rights reserved.
• US4900665A
  申请人：——

  公开号：US4900665A

  公开（公告）日：1990-02-13
• 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.