Glu-Arg | 7219-59-2

• 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: Glu-Arg
• 英文别名: Glutamylarginine；(4S)-4-amino-5-[[(1S)-1-carboxy-4-(diaminomethylideneamino)butyl]amino]-5-oxopentanoic acid
• CAS: 7219-59-2
• 化学式: C₁₁H₂₁N₅O₅
• 分子量: 303.318
• InChiKey: MPZWMIIOPAPAKE-BQBZGAKWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -5
• 重原子数：
  21
• 可旋转键数：
  10
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.64
• 拓扑面积：
  194
• 氢给体数：
  6
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  5-苄基-N-Cbz-L-谷氨酸酯 在 钯 sodium hydroxide 、 氢气 作用下， 以 甲醇 、 水 、 溶剂黄146 、 丙酮 为溶剂， 生成 Glu-Arg
  参考文献：
  名称：

  Gibian,H.; Schroeder,E., Justus Liebigs Annalen der Chemie, 1961, vol. 642, p. 145 - 162

  摘要：

  DOI：

文献信息

• Modelling of prebiotic synthesis and selection of peptides under isothermal conditions and thermal cycling mode
  作者：O. V. Demina、A. S. Kononikhin、A. V. Laptev、A. A. Khodonov、E. N. Nikolaev、S. D. Varfolomeev

  DOI：10.1007/s11172-012-0060-3

  日期：2012.2

  The model peptide synthesis from mixtures of amino acids was carried out under the thermal cycling and isothermal modes. The compositions of the obtained mixtures of products and the primary amino acid sequence of the synthesized peptides were determined by Fourier transform ion cyclotron resonance mass spectrometry and tandem mass spectrometry in combination with high-performance liquid chromatography

  氨基酸混合物的模型肽合成在热循环和等温模式下进行。通过傅里叶变换离子回旋共振质谱和串联质谱结合高效液相色谱法，应用合成肽的从头测序，确定了所得产物混合物的组成和合成肽的一级氨基酸序列。产品。与可能的统计组相比，肽的天然合成过程显示在相对温和的温度条件下发生并且产生的肽数量显着减少。系统的演变发生在固相合成过程中，一系列最不稳定的肽消失了。
• Recombinant light chains of botulinum neurotoxins and light chain fusion proteins for use in research and clinical therapy
  申请人：——

  公开号：US20020168727A1

  公开（公告）日：2002-11-14

  Botulinum neurotoxins, the most potent of all toxins, induce lethal neuromuscular paralysis by inhibiting exocytosis at the neuromuscular junction. The light chains (LC) of these dichain neurotoxins are a new class of zinc-endopeptidases that specifically cleave the synaptosomal proteins, SNAP-25, VAMP, or syntaxin at discrete sites. The present invention relates to the construction, expression, purification, and use of synthetic or recombinant botulinum neutoroxin genes. For example, a synthetic gene for the LC of the botulinum neurotoxin serotype A (BoNT/A) was constructed and overexpressed in Escherichia coli. The gene product was purified from inclusion bodies. The methods of the invention can provide 1.1 g of the LC per liter of culture. The LC product was stable in solution at 4° C. for at least 6 months. This rBoNT/A LC was proteolytically active, specifically cleaving the Glu-Arg bond in a 17-residue synthetic peptide of SNAP-25, the reported cleavage site of BoNT/A. Its calculated catalytic efficiency k cat /K m was higher than that reported for the native BoNT/A dichain. Treating the rBoNT/A LC with mercuric compounds completely abolished its activity, most probably by modifying the cysteine-164 residue located in the vicinity of the active site. About 70% activity of the LC was restored by adding Zn 2+ to a Zn 2+ -free, apo-LC preparation. The LC was nontoxic to mice and failed to elicit neutralizing epitope(s) when the animals were vaccinated with this protein. In addition, injecting rBoNT/A LC into sea urchin eggs inhibited exocytosis-dependent plasma membrane resealing.

  肉毒杆菌神经毒素是所有毒素中毒性最强的一种，它通过抑制神经肌肉接头处的外泌作用诱发致命的神经肌肉麻痹。这些二链神经毒素的轻链（LC）是一类新型锌内肽酶，可在离散位点特异性地裂解突触体蛋白、SNAP-25、VAMP 或 syntaxin。本发明涉及合成或重组肉毒杆菌神经毒素基因的构建、表达、纯化和使用。例如，构建了肉毒杆菌神经毒素血清型 A（BoNT/A）LC 的合成基因，并在 大肠杆菌中过表达。 从包涵体中纯化出基因产物。本发明的方法每升培养物可提供 1.1 克 LC。LC 产物在 4° C 的溶液中至少可稳定 6 个月。这种 rBoNT/A LC 具有蛋白水解活性，能特异性地裂解 SNAP-25 的 17 个残基合成肽中的 Glu-Arg 键，而 SNAP-25 正是已报道的 BoNT/A 的裂解位点。其计算催化效率 k cat /K m 高于报道的原生 BoNT/A 二链的催化效率。用汞化合物处理 rBoNT/A LC 会完全丧失其活性，很可能是通过改变位于活性位点附近的半胱氨酸-164 残基。加入 Zn 2&plus； 到 Zn 2&plus； -不含 Zn 2+ 的 apo-LC 制剂中添加 Zn 2+ 后，LC 的活性恢复了约 70%。这种 LC 对小鼠无毒，用这种蛋白质给动物接种疫苗时也不能诱导出中和表位。此外，将 rBoNT/A LC 注入海胆卵中可抑制依赖外泌的质膜再封闭。
• RECOMBINANT LIGHT CHAINS OF BOTULINUM NEUROTOXINS AND LIGHT CHAIN FUSION PROTEINS FOR USE IN RESEARCH AND CLINICAL THERAPY
  申请人：United States Army Medical Research and Material Command

  公开号：EP1409529A2

  公开（公告）日：2004-04-21
• US7037680B2
  申请人：——

  公开号：US7037680B2

  公开（公告）日：2006-05-02
• US7227010B2
  申请人：——

  公开号：US7227010B2

  公开（公告）日：2007-06-05