3-amino-2-hydroxypropanamide

• 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: 3-amino-2-hydroxypropanamide
• 英文别名: iso-serine amide
• 化学式: C₃H₈N₂O₂
• mdl: MFCD19207377
• 分子量: 104.109
• InChiKey: LEAQZMXPWIKGQQ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.4
• 重原子数：
  7
• 可旋转键数：
  2
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.666
• 拓扑面积：
  89.3
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  3-(3-(4-chloro-5-fluoropyrimidin-2-yl)-1-(2-fluorobenzyl)-1H-pyrazol-5-yl)isoxazole 、 3-amino-2-hydroxypropanamide 在 三乙胺 作用下， 以 1,4-二氧六环 、 水 为溶剂， 反应 6.0h， 以14%的产率得到3-[[5-Fluoro-2-[1-[(2-fluorophenyl)methyl]-5-(1,2-oxazol-3-yl)pyrazol-3-yl]pyrimidin-4-yl]amino]-2-hydroxypropanamide
  参考文献：
  名称：

  [EN] SGC STIMULATORS
  [FR] STIMULATEURS DE SGC

  摘要：

  公开号：

  WO2014144100A3
• 作为产物：
  描述：

  三甲基氰硅烷 、 N-(2-氧代乙基)氨基甲酸苄酯 生成 3-amino-2-hydroxypropanamide
  参考文献：
  名称：

  Exploitation of Subtilisin BPN‘ as Catalyst for the Synthesis of Peptides Containing Noncoded Amino Acids, Peptide Mimetics and Peptide Conjugates

  摘要：

  The ability of the serine protease subtilisin BPN' to catalyze peptide bond formation between fragments containing noncoded amino acids, peptide mimetics, and peptide conjugates in a kinetic approach was explored. It was found that the enzyme accepts numerous of these types of compounds both as acyl donor and acyl acceptor. The results together with specificity studies reported by others provide an active site model as a guideline in the design of enzymatic synthesis of biologically important compounds.

  DOI：

  10.1021/ja964399w

文献信息

• [EN] SGC STIMULATORS<br/>[FR] STIMULATEURS DE SGC
  申请人：NAKAI TAKASHI

  公开号：WO2014144100A3

  公开（公告）日：2014-11-06
• Exploitation of Subtilisin BPN‘ as Catalyst for the Synthesis of Peptides Containing Noncoded Amino Acids, Peptide Mimetics and Peptide Conjugates
  作者：Wilna J. Moree、Pamela Sears、Katsuhiro Kawashiro、Krista Witte、Chi-Huey Wong

  DOI：10.1021/ja964399w

  日期：1997.4.1

  The ability of the serine protease subtilisin BPN' to catalyze peptide bond formation between fragments containing noncoded amino acids, peptide mimetics, and peptide conjugates in a kinetic approach was explored. It was found that the enzyme accepts numerous of these types of compounds both as acyl donor and acyl acceptor. The results together with specificity studies reported by others provide an active site model as a guideline in the design of enzymatic synthesis of biologically important compounds.