methylaminoacetate | 53998-08-6

• 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: methylaminoacetate
• 英文别名: N-methyl-glycine；sarkosinate ion；methylglycinate；sarcosinate；N-methyl-glycine anion；2-(methylamino)acetate
• CAS: 53998-08-6
• 化学式: C₃H₆NO₂
• 分子量: 88.0861
• InChiKey: FSYKKLYZXJSNPZ-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -2.1
• 重原子数：
  6
• 可旋转键数：
  1
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  52.2
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  methylaminoacetate 在 Fe(CN)5NO2(4-) 、 sodium chloride 作用下， 以 水 为溶剂， 生成 alkaline earth salt of/the/ methylsulfuric acid
  参考文献：
  名称：

  The Kinetics and Mechanism of Reactions Between the Nitroprusside Ion and Secondary Amines

  摘要：

  AbstractThe kinetics of the reactions of the nitroprusside ion — pentacyanonitrosylferrate(II) — with various secondary amines have been studied in basic media. Two parallel reaction pathways are involved: (i) the reaction of the nitroprusside ion with hydroxyl ions to form Fe(CN)5NO4+2, in which NO−2 is then replaced by the amine; and (ii) the reaction of the nitroprusside ion with two molecules of amine to form the corresponding nitrosamine and the complex Fe(CN)5NHR3‐2. The corresponding rate equations have been obtained and explained by proposed reaction mechanisms. We propose a concerted mechanism for reaction (ii) in which the amine binds the nitrosyl group at the same time as the amine proton is removed by a base catalyst. The resulting nitrosamine complex subsequently undergoes substitution by the amine in a faster step.

  DOI：

  10.1002/bbpc.19850890704
• 作为产物：
  描述：

  glyoxylate 、 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 methylaminoacetate
  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

• Bunting, John W.; Stefanidis, Dimitrios, Journal of the American Chemical Society, 1990, vol. 112, # 2, p. 779 - 786
  作者：Bunting, John W.、Stefanidis, Dimitrios

  DOI：——

  日期：——
• Erickson, Luther E.; Ferrett; Buhse, Inorganic Chemistry, 1983, vol. 22, # 10, p. 1461 - 1467
  作者：Erickson, Luther E.、Ferrett、Buhse

  DOI：——

  日期：——
• Amari, Toru; Funahashi, Shigenobu; Tanaka, Motoharu, Inorganic Chemistry, 1988, vol. 27, # 19, p. 3368 - 3372
  作者：Amari, Toru、Funahashi, Shigenobu、Tanaka, Motoharu

  DOI：——

  日期：——
• 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.
• The Kinetics and Mechanism of Reactions Between the Nitroprusside Ion and Secondary Amines
  作者：J. Casado、M. Mosquera、M. F. Rodr ÍGuez Prieto、J. Vázquez Tato

  DOI：10.1002/bbpc.19850890704

  日期：1985.7

  AbstractThe kinetics of the reactions of the nitroprusside ion — pentacyanonitrosylferrate(II) — with various secondary amines have been studied in basic media. Two parallel reaction pathways are involved: (i) the reaction of the nitroprusside ion with hydroxyl ions to form Fe(CN)5NO4+2, in which NO−2 is then replaced by the amine; and (ii) the reaction of the nitroprusside ion with two molecules of amine to form the corresponding nitrosamine and the complex Fe(CN)5NHR3‐2. The corresponding rate equations have been obtained and explained by proposed reaction mechanisms. We propose a concerted mechanism for reaction (ii) in which the amine binds the nitrosyl group at the same time as the amine proton is removed by a base catalyst. The resulting nitrosamine complex subsequently undergoes substitution by the amine in a faster step.