p-nitrobenzyl N-(p-nitrobenzyloxycarbonyl)glycyl-L-α-aminopimelate | 726201-88-3

• 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: p-nitrobenzyl N-(p-nitrobenzyloxycarbonyl)glycyl-L-α-aminopimelate
• CAS: 726201-88-3
• 化学式: C₂₄H₂₆N₄O₁₁
• 分子量: 546.491
• InChiKey: AOLCCDMFKOZRME-FQEVSTJZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.6
• 重原子数：
  39.0
• 可旋转键数：
  15.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  217.31
• 氢给体数：
  3.0
• 氢受体数：
  10.0

反应信息

• 作为反应物：
  描述：

  p-nitrobenzyl N-(p-nitrobenzyloxycarbonyl)glycyl-L-α-aminopimelate 在 palladium on activated charcoal 氢气 、 碳酸氢钠 、 1-羟基苯并三唑 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 、 三氟乙酸 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 为溶剂， 20.0 ℃ 、101.33 kPa 条件下， 反应 7.0h， 生成 7-(glycyl-L-α-aminopimelyl)aminocephalosporanic acid
  参考文献：
  名称：

  The Perfect Penicillin? Inhibition of a Bacterial DD-Peptidase by Peptidoglycan-Mimetic β-Lactams

  摘要：

  6-(Glycyl-l-alpha-aminopimelyl)-aminopenicillanic acid and 7-(glycyl-l-alpha-aminopimelyl)-aminocephalosporanic acid have been synthesized as Streptomyces sp. peptidoglycan-mimetic beta-lactams. These compounds inactivate the Streptomyces R61 DD-peptidase with rate constants of 1.5 x 107 s-1 M-1 and 5.6 x 105 s-1 M-1, respectively. The former compound is thus the most effective beta-lactam inhibitor of a DD-peptidase yet described. The analogous d-alanyl-d-alanine peptide has previously been shown to react with this enzyme with comparable efficiency, kcat/Km = 8.7 x 106 s-1 M-1. These results show that, in this case at least, incorporation of a peptidoglycan-mimetic side chain into a beta-lactam greatly enhances its activity as a DD-peptidase inhibitor. This result has interesting implications for beta-lactam design.

  DOI：

  10.1021/ja048850s
• 作为产物：
  描述：

  (((4-nitrobenzyl)oxy)carbonyl)glycine 在 碳酸氢钠 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 、 二环己胺 作用下， 以 乙二醇二甲醚 、 N,N-二甲基甲酰胺 为溶剂， 反应 31.08h， 生成 p-nitrobenzyl N-(p-nitrobenzyloxycarbonyl)glycyl-L-α-aminopimelate
  参考文献：
  名称：

  The Perfect Penicillin? Inhibition of a Bacterial DD-Peptidase by Peptidoglycan-Mimetic β-Lactams

  摘要：

  6-(Glycyl-l-alpha-aminopimelyl)-aminopenicillanic acid and 7-(glycyl-l-alpha-aminopimelyl)-aminocephalosporanic acid have been synthesized as Streptomyces sp. peptidoglycan-mimetic beta-lactams. These compounds inactivate the Streptomyces R61 DD-peptidase with rate constants of 1.5 x 107 s-1 M-1 and 5.6 x 105 s-1 M-1, respectively. The former compound is thus the most effective beta-lactam inhibitor of a DD-peptidase yet described. The analogous d-alanyl-d-alanine peptide has previously been shown to react with this enzyme with comparable efficiency, kcat/Km = 8.7 x 106 s-1 M-1. These results show that, in this case at least, incorporation of a peptidoglycan-mimetic side chain into a beta-lactam greatly enhances its activity as a DD-peptidase inhibitor. This result has interesting implications for beta-lactam design.

  DOI：

  10.1021/ja048850s