19-(4-Hydroxyphenyl)nonadecanoic acid | 1191914-08-5

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: 19-(4-Hydroxyphenyl)nonadecanoic acid
• CAS: 1191914-08-5
• 化学式: C₂₅H₄₂O₃
• 分子量: 390.607
• InChiKey: IJOZORVJRYYXLX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.7
• 重原子数：
  28
• 可旋转键数：
  19
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.72
• 拓扑面积：
  57.5
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  malonyl-CoA 、 对羟基苯甲酸 在 FadD₂₂ initiation module from Mycobacterium marinum 、 Pks₁₅/1 type I polyketide synthase from Mycobacterium marinum 、 NADPH 、 三(2-羰基乙基)磷盐酸盐 、 氯化镁 、 5’-三磷酸腺苷 作用下， 反应 5.0h， 生成 17-(4-Hydroxyphenyl)heptadecanoic acid 、 19-(4-Hydroxyphenyl)nonadecanoic acid 、 21-(4-hydroxyphenyl)henicosanoic acid 、 23-(4-Hydroxyphenyl)tricosanoic acid 、 、 、 、 15-(4-hydroxy-phenyl)-pentadecanoic acid 、 11-(4-hydroxyphenyl)undecanoic acid 、 13-(4-hydroxy-phenyl)-tridecanoic acid
  参考文献：
  名称：

  Cooperation between a Coenzyme A-Independent Stand-Alone Initiation Module and an Iterative Type I Polyketide Synthase during Synthesis of Mycobacterial Phenolic Glycolipids

  摘要：

  Several Mycobacterium tuberculosis strains, Mycobacterium leprae, and other mycobacterial pathogens produce a group of small-molecule virulence factors called phenolic glycolipids (PGLs). PGLs play key roles in pathogenicity and host-pathogen interaction. Thus, elucidation of the PGL biosynthetic pathway will not only expand our understanding of natural product biosynthesis, but may also illuminate routes to novel therapeutics to afford alternative lines of defense against mycobacterial infections. In this study, we report an investigation of the enzymatic requirements for the production of long-chain p-hydroxyphenylalkanoate intermediates of PGL biosynthesis. We demonstrate a functional cooperation between a coenzyme A-independent stand-alone didomain initiation module (FadD22) and a 6-domain reducing iterative type I polyketide synthase (Pks15/1) for production of p-hydroxyphenylalkanoate intermediates in in vitro and in vivo FadD22-Pks15/1 reconstituted systems. Our results suggest that Pks15/1 is an iterative type I polyketide synthase with a relaxed control of catalytic cycle iterations, a mechanistic property that explains the origin of a characteristic alkyl chain length variability seen in mycobacterial PGLs. The FadD22-Pks15/1 reconstituted systems lay an initial foundation for future efforts to unveil the mechanism of iterative catalysis control by which the structures of the final products of Pks15/1 are defined, and to scrutinize the functional partnerships of the FadD22-Pks15/1 system with downstream enzymes of the PGL biosynthetic pathway.

  DOI：

  10.1021/ja904792q

文献信息

• Cooperation between a Coenzyme A-Independent Stand-Alone Initiation Module and an Iterative Type I Polyketide Synthase during Synthesis of Mycobacterial Phenolic Glycolipids
  作者：Weiguo He、Clifford E. Soll、Sivagami Sundaram Chavadi、Guangtao Zhang、J. David Warren、Luis E. N. Quadri

  DOI：10.1021/ja904792q

  日期：2009.11.25

  Several Mycobacterium tuberculosis strains, Mycobacterium leprae, and other mycobacterial pathogens produce a group of small-molecule virulence factors called phenolic glycolipids (PGLs). PGLs play key roles in pathogenicity and host-pathogen interaction. Thus, elucidation of the PGL biosynthetic pathway will not only expand our understanding of natural product biosynthesis, but may also illuminate routes to novel therapeutics to afford alternative lines of defense against mycobacterial infections. In this study, we report an investigation of the enzymatic requirements for the production of long-chain p-hydroxyphenylalkanoate intermediates of PGL biosynthesis. We demonstrate a functional cooperation between a coenzyme A-independent stand-alone didomain initiation module (FadD22) and a 6-domain reducing iterative type I polyketide synthase (Pks15/1) for production of p-hydroxyphenylalkanoate intermediates in in vitro and in vivo FadD22-Pks15/1 reconstituted systems. Our results suggest that Pks15/1 is an iterative type I polyketide synthase with a relaxed control of catalytic cycle iterations, a mechanistic property that explains the origin of a characteristic alkyl chain length variability seen in mycobacterial PGLs. The FadD22-Pks15/1 reconstituted systems lay an initial foundation for future efforts to unveil the mechanism of iterative catalysis control by which the structures of the final products of Pks15/1 are defined, and to scrutinize the functional partnerships of the FadD22-Pks15/1 system with downstream enzymes of the PGL biosynthetic pathway.