RRA(pT)VA | 83155-88-8

• 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: RRA(pT)VA
• 英文别名: RRA(T)VA, (T)=phosphorylated Thr；N~5~-(Diaminomethylidene)-L-ornithyl-N~5~-(diaminomethylidene)-L-ornithyl-L-alanyl-O-phosphono-L-threonyl-L-valyl-L-alanine；(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]propanoyl]amino]-3-phosphonooxybutanoyl]amino]-3-methylbutanoyl]amino]propanoic acid
• CAS: 83155-88-8
• 化学式: C₂₇H₅₃N₁₂O₁₁P
• 分子量: 752.765
• InChiKey: SFVAADUTXFBCPT-JUKXBMAYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -7.4
• 重原子数：
  51
• 可旋转键数：
  23
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.7
• 拓扑面积：
  404
• 氢给体数：
  13
• 氢受体数：
  14

反应信息

• 作为反应物：
  描述：

  RRA(pT)VA 在 NtPAP₁₂ 作用下， 生成 RRATVA
  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

• Determinants for substrate specificity of the bacterial PP2C protein phosphatase tPphA from<i>Thermosynechococcus elongatus</i>
  作者：Jiyong Su、Karl Forchhammer

  DOI：10.1111/j.1742-4658.2011.08466.x

  日期：2013.1

  Members of the Mg2+- or Mn2+-dependent protein phosphatases/PP2C-like serine/threonine phosphatases (PPM/PP2C) are abundant and widely distributed in prokaryotes and eukaryotes, where they regulate diverse signal transduction pathways. Despite low sequence conservation, the structure of their catalytic core is highly conserved except for a flexible loop termed the flap subdomain. Bacterial PPM/PP2C members without C- or N-terminal regulatory domains still recognize their substrates. Based on the crystal structure of tPphA (a PPM/PP2C member from the cyanobacterium Thermosynechococcus elongatus), variants of tPphA were generated by site-directed mutagenesis to identify substrate specificity determinants. Furthermore, a PPM/PP2C chimera containing the tPphA catalytic core and the flap subdomain of human PP2Ca was also generated. tPphA variants and the chimera were tested towards different artificial substrates and native phosphorylated PII. A binding assay combining chemical crosslinking and pull-down was designed to analyze the binding of the various phosphatase variants to phosphoprotein PII. Together, these data showed that the metal 1metal 2 cluster in the catalytic center, but not the catalytically active metal 3, is required for the binding of phosphorylated substrate. Residues outside the catalytic center are pivotal for the recognition and turnover of phosphorylated protein substrate. In particular, a histidine residue (His39) of tPphA was identified to play a specific role in protein substrate dephosphorylation. Furthermore, mutations in the variable flap subdomain can affect enzyme activity as well as substrate specificity. Structured digital abstract tPphA binds to P-II by cross-linking study (View Interaction: 1, 2, 3, 4, 5, 6, 7, 8)