[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(3R)-3-hydroxy-4-[[3-[2-(1-hydroxyethylsulfanyl)ethylamino]-3-oxopropyl]amino]-2,2-dimethyl-4-oxobutyl] hydrogen phosphate | 184765-22-8

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - S-烷基辅酶A
• 英文名称: [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(3R)-3-hydroxy-4-[[3-[2-(1-hydroxyethylsulfanyl)ethylamino]-3-oxopropyl]amino]-2,2-dimethyl-4-oxobutyl] hydrogen phosphate
• CAS: 184765-22-8
• 化学式: C₂₃H₄₀N₇O₁₇P₃S
• 分子量: 811.595
• InChiKey: IXTCYSLUNZDMHA-FBMOWMAESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -5.5
• 重原子数：
  51
• 可旋转键数：
  20
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.7
• 拓扑面积：
  392
• 氢给体数：
  10
• 氢受体数：
  22

反应信息

• 作为反应物：
  描述：

  [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(3R)-3-hydroxy-4-[[3-[2-(1-hydroxyethylsulfanyl)ethylamino]-3-oxopropyl]amino]-2,2-dimethyl-4-oxobutyl] hydrogen phosphate 在 phosphate buffer 作用下， 以 水 、 重水 为溶剂， 生成 1,1-乙二醇 、 乙醛 、 辅酶 A
  参考文献：
  名称：

  Coenzyme A Hemithioacetals as Easily Prepared Inhibitors of CoA Ester-Utilizing Enzymes

  摘要：

  Hemithioacetals are formed by reactions of coenzyme A (CoA) with aldehydes in aqueous solution. Equilibria for hemithioacetal formation with four commercially available aldehydes and rate constants for hemithioacetal dissociation have been studied. The hemithioacetals are viewed as acyl-CoA analogs having a tetrahedral center in place of the planar trigonal thioester carbonyl carbon. These compounds may serve as mimics of the tetrahedral intermediate or transition state in the reactions of acyl-CoA dependent acyltransferase enzymes. The hemithioacetal generated by reaction of CoA with formaldehyde is a poor inhibitor of chloramphenicol acetyltransferase, with a K-i more than B-fold higher than the K-m for the substrate acetyl-CoA. The hemithioacetals formed by reaction of CoA with acetaldehyde and trifluroacetaldehyde are substantially better inhibitors, with K-i values approximately 2.4-fold and 10-fold lower than the K-m values for acetyl-CoA, respectively. The hemithioacetal formed by reaction of CoA with succinic semialdehyde inhibits succinic thiokinase, with a K-i 4-fold lower than the K-m for the substrate succinyl-CoA. The CoA hemithioacetals provide a novel readily accessible new class of acyl-CoA analogs for use in mechanistic and structural studies of CoA ester-utilizing enzymes.

  DOI：

  10.1021/jo9616724
• 作为产物：
  描述：

  1,1-乙二醇 、 乙醛 、 辅酶 A 在 phosphate buffer 作用下， 以 水 、 重水 为溶剂， 生成 [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(3R)-3-hydroxy-4-[[3-[2-(1-hydroxyethylsulfanyl)ethylamino]-3-oxopropyl]amino]-2,2-dimethyl-4-oxobutyl] hydrogen phosphate
  参考文献：
  名称：

  Coenzyme A Hemithioacetals as Easily Prepared Inhibitors of CoA Ester-Utilizing Enzymes

  摘要：

  Hemithioacetals are formed by reactions of coenzyme A (CoA) with aldehydes in aqueous solution. Equilibria for hemithioacetal formation with four commercially available aldehydes and rate constants for hemithioacetal dissociation have been studied. The hemithioacetals are viewed as acyl-CoA analogs having a tetrahedral center in place of the planar trigonal thioester carbonyl carbon. These compounds may serve as mimics of the tetrahedral intermediate or transition state in the reactions of acyl-CoA dependent acyltransferase enzymes. The hemithioacetal generated by reaction of CoA with formaldehyde is a poor inhibitor of chloramphenicol acetyltransferase, with a K-i more than B-fold higher than the K-m for the substrate acetyl-CoA. The hemithioacetals formed by reaction of CoA with acetaldehyde and trifluroacetaldehyde are substantially better inhibitors, with K-i values approximately 2.4-fold and 10-fold lower than the K-m values for acetyl-CoA, respectively. The hemithioacetal formed by reaction of CoA with succinic semialdehyde inhibits succinic thiokinase, with a K-i 4-fold lower than the K-m for the substrate succinyl-CoA. The CoA hemithioacetals provide a novel readily accessible new class of acyl-CoA analogs for use in mechanistic and structural studies of CoA ester-utilizing enzymes.

  DOI：

  10.1021/jo9616724