亚麻酰基辅酵素a | 6709-57-5

• 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: 亚麻酰基辅酵素a
• 中文别名: 亚油酰基辅酶A,游离酸
• 英文名称: 9Z,12Z-octadecadienoyl coenzyme A
• 英文别名: Linoleoyl-Coenzyme A；linoleoyl-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] (9Z,12Z)-octadeca-9,12-dienethioate
• CAS: 6709-57-5
• 化学式: C₃₉H₆₆N₇O₁₇P₃S
• 分子量: 1029.98
• InChiKey: YECLLIMZHNYFCK-RRNJGNTNSA-N

物化性质

• 物理描述：
  Solid

计算性质

• 辛醇/水分配系数(LogP)：
  1.1
• 重原子数：
  67
• 可旋转键数：
  34
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.69
• 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：

  [14C(U)]-snglycerol-3-phosphate 、 亚麻酰基辅酵素a 在 乙二胺四乙酸 、 DL-dithiothreitol 、 bovie serum albumin 、 Erysimum asperum sn-glycerol-3-phosphate acyltransferase 作用下， 以 aq. buffer 为溶剂， 反应 0.17h， 生成
  参考文献：
  名称：

  Possible allostery and oligomerization of recombinant plastidial sn-glycerol-3-phosphate acyltransferase

  摘要：

  Plastidial acyl-acyl carrier protein:sn-glycerol-3-phosphate acyltransferase (GPAT; EC 2.3.1.15) catalyzes the acyl-acyl carrier protein-dependent sn-1 acylation of sn-glycerol 3-phosphate (G3P) to produce lysophosphatic acid. Functional recombinant Erysimum asperum GPAT (EaGPAT), devoid of transit peptide, was produced in yeast. Analysis of the dependence of EaGPAT activity on increasing G3P concentration resulted in a hyperbolic response. EaGPAT exhibited a preference for 18-carbon unsaturated acyl-CoAs. Assays with concentrations of oleoyl-CoA up to 90μM revealed an exponential response to increasing concentrations of acyl donor, and the introduction of increasing concentrations of unlabeled linoleoyl-CoA into the standard reaction mixture resulted in increased incorporation of radiolabeled oleoyl moieties into lysophosphatidic acid. Collectively, the kinetic results suggest that acyl-CoA may act as both substrate and allosteric effector. EaGPAT was also shown to oligomerize to form higher molecular mass multimers, with the monomer and trimer being the predominant forms of the enzyme. Since most allosteric enzyme exhibit quaternary structure, the self-associating properties of EaGPAT are consistent with those of an allosteric enzyme. These results could have important regulatory implications when plastidial GPAT is introduced into a cytoplasmic environment where acyl-CoA is the acyl donor supporting cytoplasmic glycerolipid assembly.

  DOI：

  10.1016/j.abb.2014.05.007
• 作为试剂：
  描述：

  (2R)-2,3-二羟基丙基磷酸二氢酯 、 在 乙二胺四乙酸 、 DL-dithiothreitol 、 bovie serum albumin 、 Erysimum asperum sn-glycerol-3-phosphate acyltransferase 、 亚麻酰基辅酵素a 作用下， 以 aq. buffer 为溶剂， 反应 0.17h， 生成
  参考文献：
  名称：

  Possible allostery and oligomerization of recombinant plastidial sn-glycerol-3-phosphate acyltransferase

  摘要：

  Plastidial acyl-acyl carrier protein:sn-glycerol-3-phosphate acyltransferase (GPAT; EC 2.3.1.15) catalyzes the acyl-acyl carrier protein-dependent sn-1 acylation of sn-glycerol 3-phosphate (G3P) to produce lysophosphatic acid. Functional recombinant Erysimum asperum GPAT (EaGPAT), devoid of transit peptide, was produced in yeast. Analysis of the dependence of EaGPAT activity on increasing G3P concentration resulted in a hyperbolic response. EaGPAT exhibited a preference for 18-carbon unsaturated acyl-CoAs. Assays with concentrations of oleoyl-CoA up to 90μM revealed an exponential response to increasing concentrations of acyl donor, and the introduction of increasing concentrations of unlabeled linoleoyl-CoA into the standard reaction mixture resulted in increased incorporation of radiolabeled oleoyl moieties into lysophosphatidic acid. Collectively, the kinetic results suggest that acyl-CoA may act as both substrate and allosteric effector. EaGPAT was also shown to oligomerize to form higher molecular mass multimers, with the monomer and trimer being the predominant forms of the enzyme. Since most allosteric enzyme exhibit quaternary structure, the self-associating properties of EaGPAT are consistent with those of an allosteric enzyme. These results could have important regulatory implications when plastidial GPAT is introduced into a cytoplasmic environment where acyl-CoA is the acyl donor supporting cytoplasmic glycerolipid assembly.

  DOI：

  10.1016/j.abb.2014.05.007

文献信息

• Possible allostery and oligomerization of recombinant plastidial sn-glycerol-3-phosphate acyltransferase
  作者：Xue Chen、Robin Miles、Crystal Snyder、Martin Truksa、Jian Zhang、Saleh Shah、Randall J. Weselake

  DOI：10.1016/j.abb.2014.05.007

  日期：2014.7

  Plastidial acyl-acyl carrier protein:sn-glycerol-3-phosphate acyltransferase (GPAT; EC 2.3.1.15) catalyzes the acyl-acyl carrier protein-dependent sn-1 acylation of sn-glycerol 3-phosphate (G3P) to produce lysophosphatic acid. Functional recombinant Erysimum asperum GPAT (EaGPAT), devoid of transit peptide, was produced in yeast. Analysis of the dependence of EaGPAT activity on increasing G3P concentration resulted in a hyperbolic response. EaGPAT exhibited a preference for 18-carbon unsaturated acyl-CoAs. Assays with concentrations of oleoyl-CoA up to 90μM revealed an exponential response to increasing concentrations of acyl donor, and the introduction of increasing concentrations of unlabeled linoleoyl-CoA into the standard reaction mixture resulted in increased incorporation of radiolabeled oleoyl moieties into lysophosphatidic acid. Collectively, the kinetic results suggest that acyl-CoA may act as both substrate and allosteric effector. EaGPAT was also shown to oligomerize to form higher molecular mass multimers, with the monomer and trimer being the predominant forms of the enzyme. Since most allosteric enzyme exhibit quaternary structure, the self-associating properties of EaGPAT are consistent with those of an allosteric enzyme. These results could have important regulatory implications when plastidial GPAT is introduced into a cytoplasmic environment where acyl-CoA is the acyl donor supporting cytoplasmic glycerolipid assembly.