N⁵-((R)-3-(((S)-3-amino-3-carboxypropyl)disulfanyl)-1-((carboxymethyl)amino)-1-oxopropan-2-yl)-L-glutamine | 75027-08-6

• 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: N⁵-((R)-3-(((S)-3-amino-3-carboxypropyl)disulfanyl)-1-((carboxymethyl)amino)-1-oxopropan-2-yl)-L-glutamine
• CAS: 75027-08-6
• 化学式: C₁₄H₂₄N₄O₈S₂
• 分子量: 440.499
• InChiKey: DZTIBCUOQYEROY-CIUDSAMLSA-N

物化性质

• 沸点：
  890.0±65.0 °C(Predicted)
• 密度：
  1.509±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -1.95
• 重原子数：
  28.0
• 可旋转键数：
  15.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.64
• 拓扑面积：
  222.14
• 氢给体数：
  7.0
• 氢受体数：
  9.0

反应信息

• 作为反应物：
  描述：

  L-高半胱氨酸 、 N⁵-((R)-3-(((S)-3-amino-3-carboxypropyl)disulfanyl)-1-((carboxymethyl)amino)-1-oxopropan-2-yl)-L-glutamine 在 sodium chloride 作用下， 以 重水 为溶剂， 生成 L-高胱氨酸 、 谷胱甘肽
  参考文献：
  名称：

  Kinetics and equilibria of thiol/disulfide interchange reactions of selected biological thiols and related molecules with oxidized glutathione

  摘要：

  Rate constants for reaction of coenzyme A and cysteine with oxidized glutathione (GSSG) and equilibrium constants for the reaction of coenzyme A, cysteine, homocysteine, cysteamine, and related thiols with GSSG by thiol/disulfide interchange were determined over a range of pD values by NMR spectroscopy. The rate constants for reaction of the thiolate anion forms of coenzyme A and cysteine with GSSG suggest that reduction of GSSG by coenzyme A and cysteine is a mechanistically uncomplicated S(N)2 reaction. Equilibrium constants for the thiol/disulfide interchange reactions show a strong dependence on the Bronsted basicity of the thiolate anion. In a similar way, DELTA-E-degrees', the difference between the half-cell potentials for the RSSR/RSH and GSSG/GSH redox couples, is linearly dependent on the difference between the pK(A) values of RSH and glutathione: DELTA-E-degrees' = 64-DELTA-pK(A) -7.7 where DELTA-E-degrees' is in units of mV. The reducing strength at a given pH is also determined by the fraction of the thiol present in the reactive thiolate form. At pD 7, the half-cell potentials for coenzyme A, cysteine, homocysteine, and cysteamine are close to that of glutathione, the major intracellular thiol redox system, which suggests that small changes in the intracellular redox potential can cause significant changes in the intracellular distribution of these biological thiols between their reduced and oxidized forms.

  DOI：

  10.1021/jo00027a023
• 作为产物：
  描述：

  L-高胱氨酸 、 谷胱甘肽 在 sodium chloride 作用下， 以 重水 为溶剂， 生成 L-高半胱氨酸 、 N⁵-((R)-3-(((S)-3-amino-3-carboxypropyl)disulfanyl)-1-((carboxymethyl)amino)-1-oxopropan-2-yl)-L-glutamine
  参考文献：
  名称：

  Kinetics and equilibria of thiol/disulfide interchange reactions of selected biological thiols and related molecules with oxidized glutathione

  摘要：

  Rate constants for reaction of coenzyme A and cysteine with oxidized glutathione (GSSG) and equilibrium constants for the reaction of coenzyme A, cysteine, homocysteine, cysteamine, and related thiols with GSSG by thiol/disulfide interchange were determined over a range of pD values by NMR spectroscopy. The rate constants for reaction of the thiolate anion forms of coenzyme A and cysteine with GSSG suggest that reduction of GSSG by coenzyme A and cysteine is a mechanistically uncomplicated S(N)2 reaction. Equilibrium constants for the thiol/disulfide interchange reactions show a strong dependence on the Bronsted basicity of the thiolate anion. In a similar way, DELTA-E-degrees', the difference between the half-cell potentials for the RSSR/RSH and GSSG/GSH redox couples, is linearly dependent on the difference between the pK(A) values of RSH and glutathione: DELTA-E-degrees' = 64-DELTA-pK(A) -7.7 where DELTA-E-degrees' is in units of mV. The reducing strength at a given pH is also determined by the fraction of the thiol present in the reactive thiolate form. At pD 7, the half-cell potentials for coenzyme A, cysteine, homocysteine, and cysteamine are close to that of glutathione, the major intracellular thiol redox system, which suggests that small changes in the intracellular redox potential can cause significant changes in the intracellular distribution of these biological thiols between their reduced and oxidized forms.

  DOI：

  10.1021/jo00027a023