(R)-4-methyl-tritriacontane | 149037-52-5

• 分子结构分类: 有机化合物 - 碳氢化合物 - 饱和烃
• 英文名称: (R)-4-methyl-tritriacontane
• 英文别名: (R)-4-Methyl-tritriacontan；(4R)-4-methyltritriacontane
• CAS: 149037-52-5
• 化学式: C₃₄H₇₀
• 分子量: 478.93
• InChiKey: HUWHFLXKPGENCC-UUWRZZSWSA-N

物化性质

• 熔点：
  58.6-58.7 °C
• 沸点：
  540.7±17.0 °C(Predicted)
• 密度：
  0.811±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  18.3
• 重原子数：
  34
• 可旋转键数：
  30
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  0
• 氢给体数：
  0
• 氢受体数：
  0

反应信息

• 作为产物：
  描述：

  3-氧代癸酸甲酯 在 盐酸 、 amalgamated zinc 、 溶剂黄146 、 2-戊酮 作用下， 生成 (R)-4-methyl-tritriacontane
  参考文献：
  名称：

  Long PDE4 cAMP specific phosphodiesterases are activated by protein kinase A-mediated phosphorylation of a single serine residue in Upstream Conserved Region 1 (UCR1)

  摘要：

  COS1细胞用腺苷酸环化酶激动剂 forskolin刺激导致了重组 PDE4A8、PDE4B1、PDE4C2 和 PDE4D5 cAMP特异性磷酸二酯酶长型异构体的激活。 Forskolin刺激并不会激活突变的长型 PDE4 异构体，其中蛋白激酶 A (PKA) 共识磷酸化位点上游保守区1 (UCR1) 内的丝氨酸靶点残基 (STR) 被突变为丙氨酸。 PKA抑制剂 H89 阻断了 forskolin 对野生型长型 PDE4 异构体的激活作用。 活化的 PKA 引起了重组野生型长型 PDE4 异构体的体外磷酸化，但对 STR 突变为丙氨酸的异构体无效。 British Journal of Pharmacology (2002) 136, 421–433; doi:10.1038/sj.bjp.0704743

  DOI：

  10.1038/sj.bjp.0704743

文献信息

• Long PDE4 cAMP specific phosphodiesterases are activated by protein kinase A-mediated phosphorylation of a single serine residue in Upstream Conserved Region 1 (UCR1)
  作者：Simon J MacKenzie、George S Baillie、Ian McPhee、Carolynn MacKenzie、Rachael Seamons、Theresa McSorley、Jenni Millen、Matthew B Beard、Gino van Heeke、Miles D Houslay

  DOI：10.1038/sj.bjp.0704743

  日期：2002.6

  Challenge of COS1 cells with the adenylyl cyclase activator forskolin led to the activation of recombinant PDE4A8, PDE4B1, PDE4C2 and PDE4D5 cAMP‐specific phosphodiesterase long isoforms. Forskolin challenge did not activate mutant long PDE4 isoforms where the serine target residue (STR) within the protein kinase A (PKA) consensus phosphorylation site in Upstream Conserved Region 1 (UCR1) was mutated to alanine. The PKA inhibitor, H89, ablated forskolin activation of wild‐type long PDE4 isoforms. Activated PKA caused the in vitro phosphorylation of recombinant wild‐type long PDE4 isoforms, but not those where the STR was mutated to alanine. An antiserum specific for the phosphorylated form of the STR detected a single immunoreactive band for recombinant long PDE4 isoforms expressed in COS1 cells challenged with forskolin. This was not evident in forskolin‐challenged cells treated with H89. Neither was it evident in forskolin‐challenged cells expressing long isoforms where the STR had been mutated to alanine. In transfected COS cells challenged with forskolin, only the phosphorylated PDE4D3 long form showed a decrease in mobility in Western blotting analysis. This decreased mobility of PDE4D3 was ablated upon mutation of either of the two serine targets for PKA phosphorylation in this isoform, namely Ser54 in UCR1 and Ser13 in the isoform‐specific N‐terminal region. Activation by forskolin challenge did not markedly alter the sensitivity of PDE4A8, PDE4B1, PDE4C2 and PDE4D5 to inhibition by rolipram. Long PDE4 isoforms from all four sub‐families can be phosphorylated by protein kinase A (PKA). This leads to an increase in their activity and may thus contribute to cellular desensitization processes in cells where these isoforms are selectively expressed. British Journal of Pharmacology (2002) 136, 421–433; doi:10.1038/sj.bjp.0704743

  COS1细胞用腺苷酸环化酶激动剂 forskolin刺激导致了重组 PDE4A8、PDE4B1、PDE4C2 和 PDE4D5 cAMP特异性磷酸二酯酶长型异构体的激活。 Forskolin刺激并不会激活突变的长型 PDE4 异构体，其中蛋白激酶 A (PKA) 共识磷酸化位点上游保守区1 (UCR1) 内的丝氨酸靶点残基 (STR) 被突变为丙氨酸。 PKA抑制剂 H89 阻断了 forskolin 对野生型长型 PDE4 异构体的激活作用。 活化的 PKA 引起了重组野生型长型 PDE4 异构体的体外磷酸化，但对 STR 突变为丙氨酸的异构体无效。 British Journal of Pharmacology (2002) 136, 421–433; doi:10.1038/sj.bjp.0704743