DADEYLIPQQG | 152646-18-9

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: DADEYLIPQQG
• CAS: 152646-18-9
• 化学式: C₅₄H₈₁N₁₃O₂₁
• 分子量: 1248.31
• InChiKey: MVZJYAGPPBHFFH-VZAHYZMKSA-N

物化性质

• 沸点：
  1773.1±65.0 °C(predicted)
• 密度：
  1.377±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(predicted)

反应信息

• 作为产物：
  描述：

  DADEpYLIPQQG 在 NtPAP₁₂ 作用下， 生成 DADEYLIPQQG
  参考文献：
  名称：

  Purple acid phosphatase in the walls of tobacco cells

  摘要：

  Purple acid phosphatase isolated from the walls of tobacco cells appears to be a 220 kDa homotetramer composed of 60 kDa subunits, which is purple in color and which contains iron as its only metal ion. Although the phosphatase did not require dithiothreitol for activity and was not inhibited by phenylarsine oxide, the enzyme showed a higher catalytic efficiency (k(cat)/K-m) for phosphotyrosine-containing peptides than for other substrates including p-nitrophenyl-phosphate and ATP. The phosphatase formed as a 120 kDa dimer in the cytoplasm and as a 220 kDa tetramer in the walls, where Brefeldin A blocked its secretion during wall regeneration. According to our double-immunofluorescence labeling results, the enzyme might be translocated through the Golgi apparatus to the walls at the interphase and to the cell plate during cytokinesis. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.phytochem.2008.07.008

文献信息

• Target-specific control of lymphoid-specific protein tyrosine phosphatase (Lyp) activity
  作者：Zandra E. Walton、Anthony C. Bishop

  DOI：10.1016/j.bmc.2010.06.022

  日期：2010.7

  Lymphoid-specific protein tyrosine phosphatase (Lyp), a member of the protein tyrosine phosphatase (PTP) superfamily of enzymes, is an important mediator of human-leukocyte signaling. Lyp has also emerged as a potential anti-autoimmune therapeutic target, owing to the association of a Lyp-activating mutation with an array of autoimmune disorders. Toward the goal of generating a selective inhibitor of Lyp activity that could be used for investigating Lyp's roles in cell signaling and autoimmune-disease progression, here we report that Lyp's PTP domain can be readily sensitized to target-specific inhibition by a cell-permeable small molecule. Insertion of a tetracysteine-motif-containing peptide at a conserved position in Lyp's catalytic domain generated a mutant enzyme (Lyp-CCPGCC) that retains activity comparable to that of wild-type Lyp in the absence of added ligand. Upon addition of a tetracysteine-targeting biarsenical compound (FlAsH), however, the activity of the Lyp-CCPGCC drops dramatically, as assayed with either small-molecule or phosphorylated-peptide PTP substrates. We show that FlAsH-induced Lyp-CCPGCC inhibition is potent, specific, rapid, and independent of the nature of the PTP substrate used in the inhibition assay. Moreover, we show that FlAsH can be used to specifically target overexpressed Lyp-CCPGCC in a complex proteomic mixture. Since the mammalian-cell permeability of FlAsH is well established, it is likely that FlAsH-mediated inhibition of Lyp-CCPGCC will be useful for specifically targeting Lyp activity in engineered leukocytes and autoimmune-disease models. (C) 2010 Elsevier Ltd. All rights reserved.
• Allele-specific inhibition of divergent protein tyrosine phosphatases with a single small molecule
  作者：Xin-Yu Zhang、Vincent L. Chen、Mari S. Rosen、Elizabeth R. Blair、Anna Mari Lone、Anthony C. Bishop

  DOI：10.1016/j.bmc.2008.07.053

  日期：2008.9

  A central challenge of chemical biology is the development of small-molecule tools for controlling protein activity in a target-specific manner. Such tools are particularly useful if they can be systematically applied to the members of large protein families. Here we report that protein tyrosine phosphatases can be systematically 'sensitized' to target-specific inhibition by a cell-permeable small molecule, Fluorescein Arsenical Hairpin Binder ( FlAsH), which does not inhibit any wild-type PTP investigated to date. We show that insertion of a FlAsH-binding peptide at a conserved position in the PTP catalytic-domain's WPD loop confers novel FlAsH sensitivity upon divergent PTPs. The position of the sensitizing insertion is readily identifiable from primary-sequence alignments, and we have generated FlAsH-sensitive mutants for seven different classical PTPs from six distinct subfamilies of receptor and non-receptor PTPs, including one phosphatase (PTP-PEST) whose three-dimensional catalytic-domain structure is not known. In all cases, FlAsH-mediated PTP inhibition was target-specific and potent, with inhibition constants for the seven sensitized PTPs ranging from 17 to 370 nM. Our results suggest that a substantial fraction of the PTP superfamily will be likewise sensitizable to allele-specific inhibition; FlAsH-based PTP targeting thus potentially provides a rapid, general means for selectively targeting PTP activity in cell-culture- or model-organism-based signaling studies. (C) 2008 Elsevier Ltd. All rights reserved.