(S)-2-Amino-N-ethyl-butyramide; hydrochloride | 187680-43-9

• 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: (S)-2-Amino-N-ethyl-butyramide; hydrochloride
• 英文别名: S 2-Amino-N-ethylbutyramide hydrochloride；(2S)-2-amino-N-ethylbutanamide;hydrochloride
• CAS: 187680-43-9
• 化学式: C₆H₁₄N₂O*ClH
• 分子量: 166.651
• InChiKey: HBFOAELYBQOTNE-JEDNCBNOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.28
• 重原子数：
  10
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  55.1
• 氢给体数：
  3
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  N-tert-butoxycarbonyl-α-aminobutyric acid ethylamide 在 盐酸 作用下， 以 1,4-二氧六环 为溶剂， 反应 0.5h， 以90%的产率得到(S)-2-Amino-N-ethyl-butyramide; hydrochloride
  参考文献：
  名称：

  Specificity of Lysine:N6-Hydroxylase: A Hypothesis for a Reactive Substrate Intermediate in the Catalytic Mechanism

  摘要：

  The recombinant cytoplasmic preparation of lysine: N-6-hydroxlase catalyzes the conversion of L-lysine to its N-6-hydroxy derivative when supplemented with the cofactors NADPH and FAD. A number of lysine analogs reflecting minor alterations in the inherent structural features of the amino acid as well compounds with relatively high affinity for lysine binding domains in other proteins were examined for their ability to serve as substrates of lysine: N-6-hydroxylase. These studies have revealed that the enzyme does not tolerate any change in the structural features of L-lysine, its preferred substrate, with the exception of the replacement of the CgammaH2-methylene group by sulfur, as in (S)-2-aminoethyl-L-cysteine. L-Norleucine is a potent inhibitor of the enzyme while L-norvaline and L-alpha-aminobutyric acid do not exhibit such effect, indicating the importance of a C-4 hydrophobic side chain for effective interaction with the enzyme. Among the N-alkyl amides of hydrophobic amino acids, only L-norleucine methylamide and L-alpha-aminobutyric acid ethylamide serve as moderate inhibitors of lysine : N-6-hydroxylase. Based on the enzyme's stringent substrate specificity, a mechanism involving the conversion of L-lysine to 2-aminocaprolactam prior to its oxygenation by the 4a-peroxyflavin intermediate in the catalytic cycle is proposed. (C) 1996 Academic Press, Inc.

  DOI：

  10.1006/bioo.1996.0034