N2-(N-(2-aminobenzoyl)-L-lysyl-L-seryl-L-lysyl-L-threonyl-L-lysyl-S-((2E,6E)-8-((3-benzoylbenzyl)oxy)-3,7-dimethylocta-2,6-dien-1-yl)-L-cysteinyl)-N6-(2,4-dinitrophenyl)-L-lysyl-L-isoleucyl-L-methionine | 1352297-71-2

• 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: N2-(N-(2-aminobenzoyl)-L-lysyl-L-seryl-L-lysyl-L-threonyl-L-lysyl-S-((2E,6E)-8-((3-benzoylbenzyl)oxy)-3,7-dimethylocta-2,6-dien-1-yl)-L-cysteinyl)-N6-(2,4-dinitrophenyl)-L-lysyl-L-isoleucyl-L-methionine
• CAS: 1352297-71-2
• 化学式: C₈₂H₁₂₀N₁₆O₁₉S₂
• 分子量: 1698.08
• InChiKey: FQEHTZMPZQVZTA-NPDNSZFGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.84
• 重原子数：
  119.0
• 可旋转键数：
  59.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.52
• 拓扑面积：
  568.35
• 氢给体数：
  17.0
• 氢受体数：
  25.0

反应信息

• 作为反应物：
  描述：

  N2-(N-(2-aminobenzoyl)-L-lysyl-L-seryl-L-lysyl-L-threonyl-L-lysyl-S-((2E,6E)-8-((3-benzoylbenzyl)oxy)-3,7-dimethylocta-2,6-dien-1-yl)-L-cysteinyl)-N6-(2,4-dinitrophenyl)-L-lysyl-L-isoleucyl-L-methionine 在 Ras converting enzyme 1-enriched yeast cell membranes 作用下， 生成
  参考文献：
  名称：

  Photoaffinity labeling of Ras converting enzyme using peptide substrates that incorporate benzoylphenylalanine (Bpa) residues: Improved labeling and structural implications

  摘要：

  Rce1p catalyzes the proteolytic trimming of C-terminal tripeptides from isoprenylated proteins containing CAAX-box sequences. Because Rce1p processing is a necessary component in the Ras pathway of oncogenic signal transduction, Rce1p holds promise as a potential target for therapeutic intervention. However, its mechanism of proteolysis and active site have yet to be defined. Here, we describe synthetic peptide analogues that mimic the natural lipidated Rce1p substrate and incorporate photolabile groups for photo-affinity-labeling applications. These photoactive peptides are designed to crosslink to residues in or near the Rce1p active site. By incorporating the photoactive group via p-benzoyl-L-phenylalanine (Bpa) residues directly into the peptide substrate sequence, the labeling efficiency was substantially increased relative to a previously-synthesized compound. Incorporation of biotin on the N-terminus of the peptides permitted photolabeled Rce1p to be isolated via streptavidin affinity capture. Our findings further suggest that residues outside the CAAX-box sequence are in contact with Rce1p, which has implications for future inhibitor design. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2011.10.027
• 作为产物：
  描述：

  Abz-KSKTKCK(Dnp)IM 、 (3-((((2E,6E)-8-bromo-2,6-dimethylocta-2,6-dien-1-yl)oxy)methyl)phenyl)(phenyl)methanone 在 zinc diacetate 、 三氟乙酸 作用下， 以 水 、 N,N-二甲基甲酰胺 、 正丁醇 为溶剂， 反应 2.5h， 以10%的产率得到N2-(N-(2-aminobenzoyl)-L-lysyl-L-seryl-L-lysyl-L-threonyl-L-lysyl-S-((2E,6E)-8-((3-benzoylbenzyl)oxy)-3,7-dimethylocta-2,6-dien-1-yl)-L-cysteinyl)-N6-(2,4-dinitrophenyl)-L-lysyl-L-isoleucyl-L-methionine
  参考文献：
  名称：

  Photoaffinity labeling of Ras converting enzyme using peptide substrates that incorporate benzoylphenylalanine (Bpa) residues: Improved labeling and structural implications

  摘要：

  Rce1p catalyzes the proteolytic trimming of C-terminal tripeptides from isoprenylated proteins containing CAAX-box sequences. Because Rce1p processing is a necessary component in the Ras pathway of oncogenic signal transduction, Rce1p holds promise as a potential target for therapeutic intervention. However, its mechanism of proteolysis and active site have yet to be defined. Here, we describe synthetic peptide analogues that mimic the natural lipidated Rce1p substrate and incorporate photolabile groups for photo-affinity-labeling applications. These photoactive peptides are designed to crosslink to residues in or near the Rce1p active site. By incorporating the photoactive group via p-benzoyl-L-phenylalanine (Bpa) residues directly into the peptide substrate sequence, the labeling efficiency was substantially increased relative to a previously-synthesized compound. Incorporation of biotin on the N-terminus of the peptides permitted photolabeled Rce1p to be isolated via streptavidin affinity capture. Our findings further suggest that residues outside the CAAX-box sequence are in contact with Rce1p, which has implications for future inhibitor design. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2011.10.027