甘氨酰-半胱胺 | 106463-34-7

• 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
• 中文名称: 甘氨酰-半胱胺
• 英文名称: glycyl-cysteamine
• 英文别名: glycine-(2-mercapto-ethylamide)；Glycin-(2-mercapto-aethylamid)；2-Glycylamino-aethanthiol；N-Glycyl-cysteamin；2-amino N-(2-mercaptoethyl) acetamide；2-amino N-(2-mercaptoethyl)-acetamide；2-Amino-N-(2-mercaptoethyl)acetamide；2-amino-N-(2-sulfanylethyl)acetamide
• CAS: 106463-34-7
• 化学式: C₄H₁₀N₂OS
• mdl: MFCD19203976
• 分子量: 134.202
• InChiKey: JWWHIAWPJFFJBZ-UHFFFAOYSA-N

物化性质

• 沸点：
  352.4±27.0 °C(Predicted)
• 密度：
  1.135±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -1.1
• 重原子数：
  8
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  56.1
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  甘氨酰-半胱胺 、 N-acryloyl-D-alanyl-D-alanine 在 ammonium hydroxide 作用下， 反应 48.0h， 以46%的产率得到3-(N-glycyl-cysteaminyl)propanoyl-D-alanyl-D-alanine
  参考文献：
  名称：

  Synthesis and Evaluation of New Substrate Analogues of Streptomyces R61 dd-Peptidase:  Dissection of a Specific Ligand

  摘要：

  Good substrates of the Streptomyces R61 DD-peptidase, such as glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-alanine, 1 (Anderson, J. W.; Pratt, R. F. Biochemistry 2000,39,12200-12209), contain the glycyl-L-alpha-amino-E-pimelyl side chain. A number of thia variants of this structure have been synthesized by means of a disconnection strategy whereby the appropriate thiols were reacted with either acryloyl-D-alanyl-D-alanine or haloalkanoyl-D-alanyl-D-alanines. Kinetics studies of the hydrolysis of these compounds by the R61 DD-peptidase showed that the presence of the N-terminal glycylammonium ion and the pimelyl-alpha-carboxylate are very important for efficient catalysis. The results of deletion of the C-terminal D-alanine indicate a promising direction toward new inhibitors. Shorter (one methylene less) and longer (one methylene more) analogues of 1 are also poor substrates. Molecular modeling and dynamics studies suggest that the higher mobility of the active site residues and the modified substrates in enzyme-substrate complexes may be the dominant factor in this loss of reactivity. The general conclusion is that essentially all of the structural elements of the side chain of 1 are required to produce a good substrate. This result has important implications for the design of inhibitors of DD-peptidases.

  DOI：

  10.1021/jo048885a
• 作为产物：
  描述：

  ethanethiol-N-tert-butyloxycarbonyl glycinamide 在 三乙基硅烷 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 1.5h， 生成 甘氨酰-半胱胺
  参考文献：
  名称：

  Synthesis and Evaluation of New Substrate Analogues of Streptomyces R61 dd-Peptidase:  Dissection of a Specific Ligand

  摘要：

  Good substrates of the Streptomyces R61 DD-peptidase, such as glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-alanine, 1 (Anderson, J. W.; Pratt, R. F. Biochemistry 2000,39,12200-12209), contain the glycyl-L-alpha-amino-E-pimelyl side chain. A number of thia variants of this structure have been synthesized by means of a disconnection strategy whereby the appropriate thiols were reacted with either acryloyl-D-alanyl-D-alanine or haloalkanoyl-D-alanyl-D-alanines. Kinetics studies of the hydrolysis of these compounds by the R61 DD-peptidase showed that the presence of the N-terminal glycylammonium ion and the pimelyl-alpha-carboxylate are very important for efficient catalysis. The results of deletion of the C-terminal D-alanine indicate a promising direction toward new inhibitors. Shorter (one methylene less) and longer (one methylene more) analogues of 1 are also poor substrates. Molecular modeling and dynamics studies suggest that the higher mobility of the active site residues and the modified substrates in enzyme-substrate complexes may be the dominant factor in this loss of reactivity. The general conclusion is that essentially all of the structural elements of the side chain of 1 are required to produce a good substrate. This result has important implications for the design of inhibitors of DD-peptidases.

  DOI：

  10.1021/jo048885a

文献信息

• Robustness, Entrainment, and Hybridization in Dissipative Molecular Networks, and the Origin of Life
  作者：Brian J. Cafferty、Albert S. Y. Wong、Sergey N. Semenov、Lee Belding、Samira Gmür、Wilhelm T. S. Huck、George M. Whitesides

  DOI：10.1021/jacs.9b02554

  日期：2019.5.22

  (rather than stop) these oscillations, when homogeneity in their composition does not. Specifically, multiple reactants in an amide-forming network sustain oscillation when the environment (here, the space velocity) changes, while homogeneous networks-those with fewer reactants-do not. Remarkably, a mixture of two reactants of different structure-neither of which produces oscillations individually-oscillates

  在生命起源时，简单的化学反应如何自组装成复杂、强大的网络尚不清楚。这个普遍的问题——耗散分子网络的自组装——对于理解分子和生物分子系统的复杂性从简单性的增长也很重要。在这里，我们描述了一个小的振荡有机反应网络的组成中的异质性如何维持（而不是停止）这些振荡，而当它们的组成不均匀时。具体而言，当环境（此处为空速）变化时，形成酰胺的网络中的多种反应物会维持振荡，而同质网络（反应物较少的网络）则不会。值得注意的是，两种不同结构的反应物的混合物——它们都不会单独产生振荡——在组合时会发生振荡。
• Stewart et al., Journal of Biological Chemistry, 1955, vol. 215, p. 319,325
  作者：Stewart et al.

  DOI：——

  日期：——
• Wieland; Bokelmann, Justus Liebigs Annalen der Chemie, 1952, vol. 576, p. 20,29
  作者：Wieland、Bokelmann

  DOI：——

  日期：——
• Wieland; Bokelmann, Justus Liebigs Annalen der Chemie, 1956, vol. 576, p. 20,28
  作者：Wieland、Bokelmann

  DOI：——

  日期：——
• Synthesis and Evaluation of New Substrate Analogues of <i>Streptomyces</i> R61 <scp>dd</scp>-Peptidase:  Dissection of a Specific Ligand
  作者：Rajesh Nagarajan、R. F. Pratt

  DOI：10.1021/jo048885a

  日期：2004.10.1

  Good substrates of the Streptomyces R61 DD-peptidase, such as glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-alanine, 1 (Anderson, J. W.; Pratt, R. F. Biochemistry 2000,39,12200-12209), contain the glycyl-L-alpha-amino-E-pimelyl side chain. A number of thia variants of this structure have been synthesized by means of a disconnection strategy whereby the appropriate thiols were reacted with either acryloyl-D-alanyl-D-alanine or haloalkanoyl-D-alanyl-D-alanines. Kinetics studies of the hydrolysis of these compounds by the R61 DD-peptidase showed that the presence of the N-terminal glycylammonium ion and the pimelyl-alpha-carboxylate are very important for efficient catalysis. The results of deletion of the C-terminal D-alanine indicate a promising direction toward new inhibitors. Shorter (one methylene less) and longer (one methylene more) analogues of 1 are also poor substrates. Molecular modeling and dynamics studies suggest that the higher mobility of the active site residues and the modified substrates in enzyme-substrate complexes may be the dominant factor in this loss of reactivity. The general conclusion is that essentially all of the structural elements of the side chain of 1 are required to produce a good substrate. This result has important implications for the design of inhibitors of DD-peptidases.