(S)-α-N-methylaminopropionate

• 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)-α-N-methylaminopropionate
• 英文别名: (±)-methyl-Alaninate；(S)-alpha-N-methylaminopropionate；(2S)-2-(methylamino)propanoate；(2S)-2-(methylamino)propionate；(S)-2-(methylamino)propionate；(S)-2-methylaminopropanoate；N-methyl-L-alaninate；N-methyl-alaninate；methyl-L-alaninate；methyl-alaninat；methylalaninate
• 化学式: C₄H₈NO₂
• 分子量: 102.113
• InChiKey: GDFAOVXKHJXLEI-VKHMYHEASA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -1.8
• 重原子数：
  7
• 可旋转键数：
  1
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  52.2
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  piruvate 、 甲胺 在 甘油 、 还原型辅酶II(NADPH)四钠盐 、 1,4-二巯基-2,3-丁二醇 作用下， 以 aq. phosphate buffer 为溶剂， 生成 (S)-α-N-methylaminopropionate
  参考文献：
  名称：

  Ketimine reductase/CRYM catalyzes reductive alkylamination of α-keto acids, confirming its function as an imine reductase

  摘要：

  Recently, crystalized mouse ketimine reductase/CRYM complexed with NADPH was found to have pyruvate bound in its active site. We demonstrate that the enzyme binds alpha-keto acids, such as pyruvate, in solution, and catalyzes the formation of N-alkyl-amino acids from alkylamines and alpha-keto acids (via reduction of imine intermediates), but at concentrations of these compounds not expected to be encountered in vivo. These findings confirm that, mechanistically, ketimine reductase/CRYM acts as a classical imine reductase and may explain the finding of bound pyruvate in the crystallized protein.

  DOI：

  10.1007/s00726-015-2044-8

文献信息

• Synthesis and immunological activity of water-soluble Thalidomide prodrugs
  作者：S Hess

  DOI：10.1016/s0968-0896(00)00342-4

  日期：2001.5

  A series of new water-soluble thalidomide prodrugs was prepared. All compounds were derivatized on the nitrogen of the glutarimide ring. Esters of natural amino acids and succinic acid derivatives have been introduced by reaction with the hydroxymethyl thalidomide 2. Nicotinic acid derivatives were prepared from halomethyl derivatives. Additionally, a methoxy methyl derivative and a carboxymethyl derivative were prepared directly from thalidomide. Most compounds showed a very large increase in water solubility compared to thalidomide itself (0.012 mg/mL). The amorphous hydrochlorides of the N-methylalanine ester 8, valine ester 9, and glycylglycine ester 10, respectively, were the most soluble compounds showing solubility greater than 300 mg/mL, which equals an increase greater than 15,000-fold. The lipophilicity of the prodrugs has been determined by their HPLC capacity factors k '. The stability of selected compounds was determined. The hydrolysis rates follow pseudo-first order kinetics. In order to assess the immunological activity, the prodrugs were tested using tumor necrosis factor-alpha and interleukin-2 inhibition assays. Selected compounds were additionally investigated on their abililty to inhibit the local Shwartzman reaction, an assay to determine the Vascular permeability. The prodrugs retained high effectiveness in the inhibition of TNF-alpha release. Our results indicated that the more stable prodrugs exhibited higher activity in the immunological assays. Some compounds showed higher activity than thalidomide itself, suggesting a high affine binding to the pharmacophore. In conclusion, the prodrugs exhibited high water solubility and high activity and might therefore be used in therapeutic applications. (C) 2001 Elsevier Science Ltd. All rights reserved.
• Ketimine reductase/CRYM catalyzes reductive alkylamination of α-keto acids, confirming its function as an imine reductase
  作者：André Hallen、Arthur J. L. Cooper、Jason R. Smith、Joanne F. Jamie、Peter Karuso

  DOI：10.1007/s00726-015-2044-8

  日期：2015.11

  Recently, crystalized mouse ketimine reductase/CRYM complexed with NADPH was found to have pyruvate bound in its active site. We demonstrate that the enzyme binds alpha-keto acids, such as pyruvate, in solution, and catalyzes the formation of N-alkyl-amino acids from alkylamines and alpha-keto acids (via reduction of imine intermediates), but at concentrations of these compounds not expected to be encountered in vivo. These findings confirm that, mechanistically, ketimine reductase/CRYM acts as a classical imine reductase and may explain the finding of bound pyruvate in the crystallized protein.