萘酚平-辅酶A | 112195-81-0

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 中文名称: 萘酚平-辅酶A
• 英文名称: nafenopin coenzym A
• 英文别名: Nafenopin-coenzyme A；S-[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]ethyl] 2-methyl-2-[4-(1,2,3,4-tetrahydronaphthalen-1-yl)phenoxy]propanethioate
• CAS: 112195-81-0
• 化学式: C₄₁H₅₆N₇O₁₈P₃S
• 分子量: 1059.92
• InChiKey: MUIWZLHYOXABMT-WFSMWQGZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.5
• 重原子数：
  70
• 可旋转键数：
  24
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.51
• 拓扑面积：
  398
• 氢给体数：
  9
• 氢受体数：
  23

反应信息

• 作为产物：
  描述：

  萘酚平 、 辅酶 A 在 choloyl-CoA hydrolase 、 magnesium chloride 作用下， 反应 4.0h， 生成 萘酚平-辅酶A
  参考文献：
  名称：

  Kinetic characteristics of rat liver peroxisomal nafenopin-CoA ligase

  摘要：

  In this study we have demonstrated that rat hepatic peroxisomes catalyse the formation of nafenopin-CoA The process is mediated by apparent high affinity (K-m 6.7 mu M), low capacity (V-max 0.31 nmol/mg/min) and low affinity, high capacity isoforms. Palmitic acid (K-i 1.1 mu M), R(-) ibuprofen (K-i 7.9 mu M), ciprofibrate (K-i 60.2 mu M) and clofibric acid (K-i 86.8 mu M) competitively inhibited nafenopin-CoA formation catalysed by the apparent high affinity isoform. An antibody raised against the microsomal palmitoyl-CoA ligase inhibited the equivalent peroxisomal enzyme significantly (P < 0.001) but did not inhibit peroxisomal nafenopin-CoA ligase activity. These data suggest that nafenopin-CoA formation is catalysed by a peroxisomal CoA ligase which differs from the peroxisomal long chain fatty acid-CoA ligase in relation to its xenobiotic/antibody inhibitor profile and kinetic characteristics.

  DOI：

  10.1016/0006-2952(94)00516-o

文献信息

• Kinetic characteristics of rat liver peroxisomal nafenopin-CoA ligase
  作者：Benjamin J. Roberts、John K. Macleod、Inderjit Singh、Kathleen M. Knights

  DOI：10.1016/0006-2952(94)00516-o

  日期：1995.5

  In this study we have demonstrated that rat hepatic peroxisomes catalyse the formation of nafenopin-CoA The process is mediated by apparent high affinity (K-m 6.7 mu M), low capacity (V-max 0.31 nmol/mg/min) and low affinity, high capacity isoforms. Palmitic acid (K-i 1.1 mu M), R(-) ibuprofen (K-i 7.9 mu M), ciprofibrate (K-i 60.2 mu M) and clofibric acid (K-i 86.8 mu M) competitively inhibited nafenopin-CoA formation catalysed by the apparent high affinity isoform. An antibody raised against the microsomal palmitoyl-CoA ligase inhibited the equivalent peroxisomal enzyme significantly (P < 0.001) but did not inhibit peroxisomal nafenopin-CoA ligase activity. These data suggest that nafenopin-CoA formation is catalysed by a peroxisomal CoA ligase which differs from the peroxisomal long chain fatty acid-CoA ligase in relation to its xenobiotic/antibody inhibitor profile and kinetic characteristics.