1-(Boc-amino)cyclopropane-1-carboxylic acid N-hydroxysuccinimide ester | 90471-63-9

• 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: 1-(Boc-amino)cyclopropane-1-carboxylic acid N-hydroxysuccinimide ester
• 英文别名: 1-tert-Butoxycarbonylamino-cyclopropanecarboxylic acid 2,5-dioxo-pyrrolidin-1-yl ester；(2,5-dioxopyrrolidin-1-yl) 1-[(2-methylpropan-2-yl)oxycarbonylamino]cyclopropane-1-carboxylate
• CAS: 90471-63-9
• 化学式: C₁₃H₁₈N₂O₆
• 分子量: 298.296
• InChiKey: BHWDAMBXYOIWET-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.3
• 重原子数：
  21
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.69
• 拓扑面积：
  102
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  1-(Boc-amino)cyclopropane-1-carboxylic acid N-hydroxysuccinimide ester 在 盐酸羟胺 、 三乙胺 作用下， 以 1,4-二氧六环 、 N,N-二甲基甲酰胺 为溶剂， 以60%的产率得到1-(Boc-amino)cyclopropane-1-carboxylic hydroxamate
  参考文献：
  名称：

  Ethylene biosynthesis. 12. Analog approach to the active site topography of the ethylene-forming enzyme. Novel hydroxamate inhibitors

  摘要：

  In order to understand both the substrate specificity and active site topography of the ethylene-forming enzyme (EFE), a number of analogs of its substrate, 1-aminocyclopropanecarboxylic acid, have been prepared and studied as inhibitors. Because of the dependence of EFE activity on iron, hydroxamic acids, a functional group known to bind iron tightly, derived from several small carboxylic/amino acids were studied along with the parent amino acids. The activity of these materials was assayed in vitro against the purified EFE from apple fruit. The varying potency of the amino acid hydroxamates suggests that they do not act simply by binding to iron and removing it from the enzyme. The order of their potency was consistent with the idea that binding reflects both metal chelation and hydrophobic interactions in the active site. The most potent inhibitor, ACC-hydroxamate, has about 1 mu M K-i.

  DOI：

  10.1021/jo00123a012
• 作为产物：
  描述：

  二碳酸二叔丁酯 在 sodium hydroxide 、 N,N'-二环己基碳二亚胺 作用下， 以 1,4-二氧六环 为溶剂， 反应 34.0h， 生成 1-(Boc-amino)cyclopropane-1-carboxylic acid N-hydroxysuccinimide ester
  参考文献：
  名称：

  Ethylene biosynthesis. 12. Analog approach to the active site topography of the ethylene-forming enzyme. Novel hydroxamate inhibitors

  摘要：

  In order to understand both the substrate specificity and active site topography of the ethylene-forming enzyme (EFE), a number of analogs of its substrate, 1-aminocyclopropanecarboxylic acid, have been prepared and studied as inhibitors. Because of the dependence of EFE activity on iron, hydroxamic acids, a functional group known to bind iron tightly, derived from several small carboxylic/amino acids were studied along with the parent amino acids. The activity of these materials was assayed in vitro against the purified EFE from apple fruit. The varying potency of the amino acid hydroxamates suggests that they do not act simply by binding to iron and removing it from the enzyme. The order of their potency was consistent with the idea that binding reflects both metal chelation and hydrophobic interactions in the active site. The most potent inhibitor, ACC-hydroxamate, has about 1 mu M K-i.

  DOI：

  10.1021/jo00123a012

文献信息

• Ethylene biosynthesis. 12. Analog approach to the active site topography of the ethylene-forming enzyme. Novel hydroxamate inhibitors
  作者：Michael C. Pirrung、Jun Cao、Jrlung Chen

  DOI：10.1021/jo00123a012

  日期：1995.9

  In order to understand both the substrate specificity and active site topography of the ethylene-forming enzyme (EFE), a number of analogs of its substrate, 1-aminocyclopropanecarboxylic acid, have been prepared and studied as inhibitors. Because of the dependence of EFE activity on iron, hydroxamic acids, a functional group known to bind iron tightly, derived from several small carboxylic/amino acids were studied along with the parent amino acids. The activity of these materials was assayed in vitro against the purified EFE from apple fruit. The varying potency of the amino acid hydroxamates suggests that they do not act simply by binding to iron and removing it from the enzyme. The order of their potency was consistent with the idea that binding reflects both metal chelation and hydrophobic interactions in the active site. The most potent inhibitor, ACC-hydroxamate, has about 1 mu M K-i.