S-[2-[3-[[(2R)-4-[[[(2R,3R,5R)-5-(6-氨基嘌呤-9-基)-4-羟基-3-膦酰氧基四氢呋喃-2-基]甲氧基-羟基磷酰]氧基-羟基磷酰]氧基-2-羟基-3,3-二甲基丁酰基]氨基]丙酰氨基]乙基](5Z,8Z,11Z,14Z)-二十-5,8,11,14-四烯硫代酸 | 17046-56-9

• 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: S-[2-[3-[[(2R)-4-[[[(2R,3R,5R)-5-(6-氨基嘌呤-9-基)-4-羟基-3-膦酰氧基四氢呋喃-2-基]甲氧基-羟基磷酰]氧基-羟基磷酰]氧基-2-羟基-3,3-二甲基丁酰基]氨基]丙酰氨基]乙基](5Z,8Z,11Z,14Z)-二十-5,8,11,14-四烯硫代酸
• 英文名称: 5Z,8Z,11Z,14Z-eicosatetraenoyl coenzyme A
• 英文别名: arachidonoyl-CoA；arachidonyl-CoA；Arachidonoyl coenzyme A；C20:4-CoA；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] (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenethioate
• CAS: 17046-56-9
• 化学式: C₄₁H₆₆N₇O₁₇P₃S
• 分子量: 1054.0
• InChiKey: JDEPVTUUCBFJIW-YQVDHACTSA-N

物化性质

• 密度：
  1.47±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.9
• 重原子数：
  69
• 可旋转键数：
  34
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.61
• 拓扑面积：
  389
• 氢给体数：
  9
• 氢受体数：
  22

反应信息

• 作为反应物：
  描述：

  S-[2-[3-[[(2R)-4-[[[(2R,3R,5R)-5-(6-氨基嘌呤-9-基)-4-羟基-3-膦酰氧基四氢呋喃-2-基]甲氧基-羟基磷酰]氧基-羟基磷酰]氧基-2-羟基-3,3-二甲基丁酰基]氨基]丙酰氨基]乙基](5Z,8Z,11Z,14Z)-二十-5,8,11,14-四烯硫代酸 在 nuclease P₁ 作用下， 生成 arachidonoyl-3'-dephosphoCoA
  参考文献：
  名称：

  Inhibition of UDP-glucuronosyltransferase activity by fatty acyl-CoA

  摘要：

  We previously identified and purified UDP-glucuronosyltransferase (UGT) isoforms as targets of protein acylation from rat liver microsomes (Yamashita et al., Biochem J 312: 301-308, 1995). The acylation of UGT isoforms occurred upon incubation with acyl-CoA without another protein acyltransferase, suggesting that it was autoacylation. The study revealed the interaction of UGT isoforms with acyl-CoA. In the present study, the effects of fatty acyl-CoA on UGT activities were examined thoroughly, using a rat liver microsomal and purified enzyme fractions. The UGT activities of both fractions were inhibited by acyl-CoA in a concentration-dependent manner. The effect of acyl-CoA was observed on the activities toward various substrates, suggesting that the effect shows the wide spectrum of the isoforms of UGT. To assess the mechanism underlying the inhibition of UGT activity by acyl-CoA, the relationship of the inhibition, acyl-CoA binding to the proteins, and changes in the tertiary structure of the enzyme were examined. The kinetics of these phenomena were related closely with each other. Furthermore, the inhibition of UGT activity was specified for acyl-CoA, though a structurally related compound, acyl-3'-dephosphoCoA, had no inhibitory effect. The results suggested that the specific binding of acyl-CoA to UGT isoforms induced conformational changes of the enzymes and resultant inhibition of UGT activity. (C) 1997 Elsevier Science Inc.

  DOI：

  10.1016/s0006-2952(96)00793-9

文献信息

• CGI-58/ABHD5 is a coenzyme A-dependent lysophosphatidic acid acyltransferase
  作者：Gabriela Montero-Moran、Jorge M. Caviglia、Derek McMahon、Alexis Rothenberg、Vidya Subramanian、Zhi Xu、Samuel Lara-Gonzalez、Judith Storch、George M. Carman、Dawn L. Brasaemle

  DOI：10.1194/jlr.m001917

  日期：2010.4

  Mutations in human CGI-58/ABHD5 cause Chanarin-Dorfman syndrome (CDS), characterized by excessive storage of triacylglycerol in tissues. CGI-58 is an alpha/beta-hydrolase fold enzyme expressed in all vertebrates. The carboxyl terminus includes a highly conserved consensus sequence (HXXXXD) for acyltransferase activity. Mouse CGI-58 was expressed in Escherichia coli as a fusion protein with two amino terminal 6-histidine tags. Recombinant CGI-58 displayed acyl-CoA-dependent acyltransferase activity to lysophosphatidic acid, but not to other lysophospholipid or neutral glycerolipid acceptors. Production of phosphatidic acid increased with time and increasing concentrations of recombinant CGI-58 and was optimal between pH 7.0 and 8.5. The enzyme showed saturation kinetics with respect to 1-oleoyl-lysophosphatidic acid and oleoyl-CoA and preference for arachidonoyl-CoA and oleoyl-CoA. The enzyme showed slight preference for 1-oleoyl lysophosphatidic acid over 1-palmitoyl, 1-stearoyl, or 1-arachidonoyl lysophosphatidic acid. Recombinant CGI-58 showed intrinsic fluorescence for tryptophan that was quenched by the addition of 1-oleoyl-lysophosphatidic acid, oleoyl-CoA, arachidonoyl-CoA, and palmitoyl-CoA, but not by lysophosphatidyl choline. Expression of CGI-58 in fibroblasts from humans with CDS increased the incorporation of radiolabeled fatty acids released from the lipolysis of stored triacylglycerols into phospholipids. CGI-58 is a CoA-dependent lysophosphatidic acid acyltransferase that channels fatty acids released from the hydrolysis of stored triacylglycerols into phospholipids.-Montero-Moran, G., J. M. Caviglia, D. McMahon, A. Rothenberg, V. Suramanian, Z. Xu, S. Lara-Gonzalez, J. Storch, G. M. Carman, and D. L. Brasaemle. CGI-58/ABHD5 is a coenzyme A-dependent lysophosphatidic acid acyltransferase. J. Lipid Res. 2010. 51: 709-719.
• Inhibition of UDP-glucuronosyltransferase activity by fatty acyl-CoA
  作者：Atsushi Yamashita、Tomonari Nagatsuka、Masanobu Watanabe、Hironori Kondo、Takayuki Sugiura、Keizo Waku

  DOI：10.1016/s0006-2952(96)00793-9

  日期：1997.2

  We previously identified and purified UDP-glucuronosyltransferase (UGT) isoforms as targets of protein acylation from rat liver microsomes (Yamashita et al., Biochem J 312: 301-308, 1995). The acylation of UGT isoforms occurred upon incubation with acyl-CoA without another protein acyltransferase, suggesting that it was autoacylation. The study revealed the interaction of UGT isoforms with acyl-CoA. In the present study, the effects of fatty acyl-CoA on UGT activities were examined thoroughly, using a rat liver microsomal and purified enzyme fractions. The UGT activities of both fractions were inhibited by acyl-CoA in a concentration-dependent manner. The effect of acyl-CoA was observed on the activities toward various substrates, suggesting that the effect shows the wide spectrum of the isoforms of UGT. To assess the mechanism underlying the inhibition of UGT activity by acyl-CoA, the relationship of the inhibition, acyl-CoA binding to the proteins, and changes in the tertiary structure of the enzyme were examined. The kinetics of these phenomena were related closely with each other. Furthermore, the inhibition of UGT activity was specified for acyl-CoA, though a structurally related compound, acyl-3'-dephosphoCoA, had no inhibitory effect. The results suggested that the specific binding of acyl-CoA to UGT isoforms induced conformational changes of the enzymes and resultant inhibition of UGT activity. (C) 1997 Elsevier Science Inc.