N-δ-allyl-L-glutamine | 90346-29-5

• 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: N-δ-allyl-L-glutamine
• 英文别名: N-(γ-L-glutamyl)allylamine；N⁵-allyl-L-glutamine；N-2-Propen-1-yl-L-glutamine；(2S)-2-amino-5-oxo-5-(prop-2-enylamino)pentanoic acid
• CAS: 90346-29-5
• 化学式: C₈H₁₄N₂O₃
• 分子量: 186.211
• InChiKey: NJUABLKMOHNCQW-LURJTMIESA-N

物化性质

• 沸点：
  439.2±45.0 °C(Predicted)
• 密度：
  1.161±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -3.3
• 重原子数：
  13
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  92.4
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  N-邻苯二甲酰-L-谷氨酸酐 在 sodium carbonate 、 一水合肼 、 三乙胺 作用下， 以 四氢呋喃 、 水 为溶剂， 反应 6.0h， 生成 N-δ-allyl-L-glutamine
  参考文献：
  名称：

  Glutamine analogues as potential antimalarials

  摘要：

  Various N-substituted derivatives of glutamine, asparagine, glutaramic, succinamic and maleamic acids have been synthesized and tested in vitro against Plasmodium falciparum. From these compounds, only the glutamine derivatives (1-3) were found to have low activity. Kinetic evaluation of 1-3 revealed that these compounds also act as competitive inhibitors of gamma-glutamyl transpeptidase (EC 2.3.2.2).

  DOI：

  10.1016/0223-5234(91)90030-q

文献信息

• A Novel Catalytic Ability of γ-Glutamylcysteine Synthetase of<i>Escherichia coli</i>and Its Application in Theanine Production
  作者：Koichiro MIYAKE、Shingo KAKITA

  DOI：10.1271/bbb.90538

  日期：2009.12.23

  γ-Glutamylcysteine synthetase (γGCS, EC 6.3.2.2) catalyzes the formation of γ-glutamylcysteine from l-glutamic acid (Glu) and l-cysteine (Cys) in an ATP-dependent manner. While γGCS can use various amino acids as substrate, little is known about whether it can use non-amino acid compounds in place of Cys. We determined that γGCS from Escherichia coli has the ability to combine Glu and amines to form γ-glutamylamides. The reaction rate depended on the length of the methylene chain of the amines in the following order: n-propylamine > butylamine > ethylamine >> methylamine. The optimal pH for the reaction was narrower and more alkaline than for the reaction with an amino acid. The newly found catalytic ability of γGCS was used in the production of theanine (γ-glutamylethylamine). The resting cells of E. coli expressing γGCS, in which ATP was regenerated through glycolysis, synthesized 12.1 mm theanine (18 h) from 429 mm ethylamine.

  γ-谷氨酰半胱氨酸合成酶（γGCS，EC 6.3.2.2）以 ATP 依赖性方式催化 l-谷氨酸（Glu）和 l-半胱氨酸（Cys）形成γ-谷氨酰半胱氨酸。虽然γGCS可以使用多种氨基酸作为底物，但人们对它是否可以使用非氨基酸化合物代替Cys知之甚少。我们确定大肠杆菌中的γGCS能够将Glu和胺结合形成γ-谷氨酰胺。反应速率取决于胺的亚甲基链长度，顺序如下：正丙胺 > 丁胺 > 乙胺 >> 甲胺。与与氨基酸反应相比，该反应的最佳 pH 值更窄、碱性更强。新发现的 γGCS 催化能力被用于生产茶氨酸（γ-谷氨酰乙胺）。表达 γGCS 的大肠杆菌静息细胞通过糖酵解再生 ATP，在 18 小时内从 429 毫米乙胺中合成了 12.1 毫米茶氨酸。
• Barzily et al., 1955, vol. 5, p. 155
  作者：Barzily et al.

  DOI：——

  日期：——
• PLANTS HAVING ENHANCED YIELD-RELATED TRAITS AND A METHOD FOR MAKING THE SAME
  申请人：BASF Plant Science GmbH

  公开号：EP2304037A1

  公开（公告）日：2011-04-06
• [EN] PLANTS HAVING ENHANCED YIELD-RELATED TRAITS AND A METHOD FOR MAKING THE SAME<br/>[FR] PLANTES AYANT DES CARACTÈRES LIÉS AU RENDEMENT AMÉLIORÉS ET PROCÉDÉ POUR PRODUIRE CELLES-CI
  申请人：BASF PLANT SCIENCE GMBH

  公开号：WO2009156360A1

  公开（公告）日：2009-12-30

  The present invention relates generally to the field of molecular biology and concerns a method for enhancing various plant yield-related traits by modulating expression in a plant of a nucleic acid encoding a RHL1 (Root Hairless 1). The present invention also concerns plants having modulated expression of a nucleic acid encoding a RHL1, which plants have enhanced various plant yield-related relative to corresponding wild type plants or other control plants. The invention also provides constructs useful in the methods of the invention.
• Glutamine analogues as potential antimalarials
  作者：M Azoulay、M Vilmont、F Frappier

  DOI：10.1016/0223-5234(91)90030-q

  日期：1991.3

  Various N-substituted derivatives of glutamine, asparagine, glutaramic, succinamic and maleamic acids have been synthesized and tested in vitro against Plasmodium falciparum. From these compounds, only the glutamine derivatives (1-3) were found to have low activity. Kinetic evaluation of 1-3 revealed that these compounds also act as competitive inhibitors of gamma-glutamyl transpeptidase (EC 2.3.2.2).