L-Selenocystathionin | 23809-95-2

• 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: L-Selenocystathionin
• 英文别名: (2S)-2-ammonio-4-{[(2R)-2-ammonio-2-carboxylatoethyl]selanyl}butanoate；(2S)-2-azaniumyl-4-[(2R)-2-azaniumyl-2-carboxylatoethyl]selanylbutanoate
• CAS: 23809-95-2
• 化学式: C₇H₁₄N₂O₄Se
• 分子量: 269.159
• InChiKey: ZNWYDQPOUQRDLY-WHFBIAKZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.26
• 重原子数：
  14
• 可旋转键数：
  7
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  127
• 氢给体数：
  4
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  水 、 L-Selenocystathionin 生成 2-oxobutanoate 、 硒代-L-半胱氨酸 、 铵
  参考文献：
  名称：

  Enzymic synthesis of selenocysteine in rat liver

  摘要：

  We have investigated selenocysteine (2-amino-3-hydroselenopropionic acid) synthesis with cystathionine beta-synthase (EC 4.2.1.22) and cystathionine gamma-lyase (EC 4.4.1.1) of rat liver. When selenohomocysteine and serine were incubated with cystathionine beta-synthase, selenocystathionine was formed at a rate of 69% of that of cystathionine synthesis. Cystathionine gamma-lyase catalyzed alpha, gamma elimination of selenocystathionine to yield alpha-ketobutyrate, selenocysteine, and NH3. The reaction rate was about 3 times higher than that of cystathionine elimination. Cystathionine beta-synthase, however, did not catalyze direct formation of selenocysteine from serine and H2Se. Thus, selenocysteine is synthesized from selenohomocysteine and cystathionine beta-synthase and cystathionine gamma-lyase reactions. We confirmed this synthetic pathway also with a mixture of both enzymes and with a homogenate of rat liver.

  DOI：

  10.1021/bi00518a039
• 作为产物：
  描述：

  (S)-2-Benzyloxycarbonylamino-4-((R)-2-benzyloxycarbonylamino-2-dicyclohexylmethoxycarbonyl-ethylselanyl)-butyric acid; compound with dicyclohexyl-amine 生成 L-Selenocystathionin
  参考文献：
  名称：

  具有光学活性硒高半胱氨酸骨架的氨基酸的合成及其在肽化学中的应用。

  摘要：

  DOI：

  10.1021/jo00830a040

文献信息

• Synthesis and application in peptide chemistry of amino acids possessing an optically active selenohomocysteine skeleton
  作者：Chandra S. Pande、Jack Rudick、Roderich Walter

  DOI：10.1021/jo00830a040

  日期：1970.5
• Enzymic synthesis of selenocysteine in rat liver
  作者：Nobuyoshi Esaki、Takeshi Nakamura、Hidehiko Tanaka、Tetsuya Suzuki、Yoshimasa Morino、Kenji Soda

  DOI：10.1021/bi00518a039

  日期：1981.7.21

  We have investigated selenocysteine (2-amino-3-hydroselenopropionic acid) synthesis with cystathionine beta-synthase (EC 4.2.1.22) and cystathionine gamma-lyase (EC 4.4.1.1) of rat liver. When selenohomocysteine and serine were incubated with cystathionine beta-synthase, selenocystathionine was formed at a rate of 69% of that of cystathionine synthesis. Cystathionine gamma-lyase catalyzed alpha, gamma elimination of selenocystathionine to yield alpha-ketobutyrate, selenocysteine, and NH3. The reaction rate was about 3 times higher than that of cystathionine elimination. Cystathionine beta-synthase, however, did not catalyze direct formation of selenocysteine from serine and H2Se. Thus, selenocysteine is synthesized from selenohomocysteine and cystathionine beta-synthase and cystathionine gamma-lyase reactions. We confirmed this synthetic pathway also with a mixture of both enzymes and with a homogenate of rat liver.