辅酶 alpha-谷胱甘肽混合物二硫化物 | 6477-52-7

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 烷基辅酶A二硫化物
• 中文名称: 辅酶 alpha-谷胱甘肽混合物二硫化物
• 中文别名: 辅酶alpha-谷胱甘肽混合物二硫化物
• 英文名称: coenzyme A-glutathione mixed disulfide
• 英文别名: CoASSG；(2S)-2-amino-5-[[(2R)-3-[2-[3-[[(2R)-4-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-2-hydroxy-3,3-dimethylbutanoyl]amino]propanoylamino]ethyldisulfanyl]-1-(carboxymethylamino)-1-oxopropan-2-yl]amino]-5-oxopentanoic acid
• CAS: 6477-52-7
• 化学式: C₃₁H₅₁N₁₀O₂₂P₃S₂
• 分子量: 1072.85
• InChiKey: JYKWMJBUIXNJOG-QEWSFFBISA-N

物化性质

• 密度：
  1.91±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -10.4
• 重原子数：
  68
• 可旋转键数：
  30
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.65
• 拓扑面积：
  556
• 氢给体数：
  14
• 氢受体数：
  29

反应信息

• 作为反应物：
  描述：

  辅酶 alpha-谷胱甘肽混合物二硫化物 、 辅酶 A 在 sodium chloride 作用下， 以 重水 为溶剂， 生成 谷胱甘肽 、 辅酶A二硫醚
  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-谷胱甘肽 (氧化型) 、 辅酶 A 在 sodium chloride 作用下， 以 重水 为溶剂， 生成 谷胱甘肽 、 辅酶 alpha-谷胱甘肽混合物二硫化物
  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

文献信息

• Kinetics and equilibria of thiol/disulfide interchange reactions of selected biological thiols and related molecules with oxidized glutathione
  作者：David A. Keire、Erin Strauss、Wei Guo、Bela Noszal、Dallas L. Rabenstein

  DOI：10.1021/jo00027a023

  日期：1992.1

  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.