2-Amino-2-(2-hydroxy-ethyl)-pent-4-enoic acid | 872983-37-4

• 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: 2-Amino-2-(2-hydroxy-ethyl)-pent-4-enoic acid
• 英文别名: 2-Prop-2-en-1-ylhomoserine；2-amino-2-(2-hydroxyethyl)pent-4-enoic acid
• CAS: 872983-37-4
• 化学式: C₇H₁₃NO₃
• 分子量: 159.185
• InChiKey: SPGMLVNLSSACNB-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.8
• 重原子数：
  11
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.57
• 拓扑面积：
  83.6
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  2-Amino-2-(2-hydroxy-ethyl)-pent-4-enoic acid 在 palladium on activated charcoal 咪唑 、 盐酸 、 lithium hydroxide 、 2-苯基苯并恶唑 、 氢气 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 三乙胺 、 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 、 甲醇 、 二氯甲烷 、 水 为溶剂， 反应 30.0h， 生成 [(1S)-1-((1S)-1-{1-benzylcarbamoyl-1-[2-(tert-butyldiphenylsiloxy)ethyl]butylcarbamoyl}-2-phenylethylcarbamoyl)ethyl]carbamic acid benzyl ester
  参考文献：
  名称：

  Engineering d-amino acid containing novel protease inhibitors using catalytic site architecture

  摘要：

  The mechanism of proteolysis by serine proteases is a reasonably well-understood process. Typically, a histidine residue acting as a general base deprotonates the catalytic serine residue and the hydrolytic water molecule. We disclose here, the use of an unnatural D-amino acid as a strategic residue in P1 position, designed de novo based on the architecture of the protease catalytic site to impede the catalytic histidine residue at the stage of acyl-enzyme intermediate. Several probe molecules containing D-homoserine or its derivatives at P1 position are evaluated. Compounds 1, 6, and 8-10 produced up to 57% loss of activity against chymotrypsin. More potent and specific inhibitors could be designed with structure optimization as this strategy is completely general and can be used to design inhibitors against any serine or cysteine protease. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2005.08.019
• 作为产物：
  描述：

  在 sodium hydroxide 作用下， 反应 16.0h， 生成 2-Amino-2-(2-hydroxy-ethyl)-pent-4-enoic acid
  参考文献：
  名称：

  Engineering d-amino acid containing novel protease inhibitors using catalytic site architecture

  摘要：

  The mechanism of proteolysis by serine proteases is a reasonably well-understood process. Typically, a histidine residue acting as a general base deprotonates the catalytic serine residue and the hydrolytic water molecule. We disclose here, the use of an unnatural D-amino acid as a strategic residue in P1 position, designed de novo based on the architecture of the protease catalytic site to impede the catalytic histidine residue at the stage of acyl-enzyme intermediate. Several probe molecules containing D-homoserine or its derivatives at P1 position are evaluated. Compounds 1, 6, and 8-10 produced up to 57% loss of activity against chymotrypsin. More potent and specific inhibitors could be designed with structure optimization as this strategy is completely general and can be used to design inhibitors against any serine or cysteine protease. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2005.08.019

文献信息

• Engineering d-amino acid containing novel protease inhibitors using catalytic site architecture
  作者：Subhash C. Annedi、Farooq Biabani、Ewa Poduch、Baskar M. Mannargudi、Kanchana Majumder、Lianhu Wei、Reza Khayat、Liang Tong、Lakshmi P. Kotra

  DOI：10.1016/j.bmc.2005.08.019

  日期：2006.1

  The mechanism of proteolysis by serine proteases is a reasonably well-understood process. Typically, a histidine residue acting as a general base deprotonates the catalytic serine residue and the hydrolytic water molecule. We disclose here, the use of an unnatural D-amino acid as a strategic residue in P1 position, designed de novo based on the architecture of the protease catalytic site to impede the catalytic histidine residue at the stage of acyl-enzyme intermediate. Several probe molecules containing D-homoserine or its derivatives at P1 position are evaluated. Compounds 1, 6, and 8-10 produced up to 57% loss of activity against chymotrypsin. More potent and specific inhibitors could be designed with structure optimization as this strategy is completely general and can be used to design inhibitors against any serine or cysteine protease. (c) 2005 Elsevier Ltd. All rights reserved.