| 1415990-02-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• CAS: 1415990-02-1
• 化学式: C₁₉H₁₆O₆
• 分子量: 340.332
• InChiKey: UHGDYISIMKILPP-VQIMIIECSA-N

反应信息

• 作为反应物：
  描述：

  在 CabV 、 NADPH-dependent flavoprotein hydroxylase CabE 、 NADPH-dependent flavoprotein hydroxylase PgaE 、 NADPH-dependent flavoprotein hydroxylase UrdE 、 氧气 、 还原型辅酶II(NADPH)四钠盐 作用下， 生成 gaudimycin C
  参考文献：
  名称：

  Tailoring Enzymes Involved in the Biosynthesis of Angucyclines Contain Latent Context-Dependent Catalytic Activities

  摘要：

  Comparison of homologous angucycline modification enzymes from five closely related Streptomyces pathways (pga, cab, lad, urd, lan) allowed us to deduce the biosynthetic steps responsible for the three alternative outcomes: gaudimycin C, dehydrorabelomycin, and 11-deoxylandomycinone. The C-12b-hydroxylated urdamycin and gaudimycin metabolites appear to be the ancestral representatives from which landomycins and jadomysins have evolved as a result of functional divergence of the ketoreductase LanV and hydroxylase JadH, respectively. Specifically, LanV has acquired affinity for an earlier biosynthetic intermediate resulting in a switch in biosynthetic order and lack of hydroxyls at C-4a and C-12b, whereas in JadH, C-4a/C-12b dehydration has evolved into an independent secondary function replacing C-12b hydroxylation. Importantly, the study reveals that many of the modification enzymes carry several alternative, hidden, or ancestral catalytic functions, which are strictly dependent on the biosynthetic context.

  DOI：

  10.1016/j.chembiol.2012.04.010
• 作为产物：
  描述：

  prejadomycin 在 NADPH-dependent flavoprotein hydroxylase CabE 、 NADPH-dependent flavoprotein hydroxylase LanE 、 NADPH-dependent flavoprotein hydroxylase PgaE 、 NADPH-dependent flavoprotein hydroxylase UrdE 、 氧气 、 还原型辅酶II(NADPH)四钠盐 作用下， 生成
  参考文献：
  名称：

  Tailoring Enzymes Involved in the Biosynthesis of Angucyclines Contain Latent Context-Dependent Catalytic Activities

  摘要：

  Comparison of homologous angucycline modification enzymes from five closely related Streptomyces pathways (pga, cab, lad, urd, lan) allowed us to deduce the biosynthetic steps responsible for the three alternative outcomes: gaudimycin C, dehydrorabelomycin, and 11-deoxylandomycinone. The C-12b-hydroxylated urdamycin and gaudimycin metabolites appear to be the ancestral representatives from which landomycins and jadomysins have evolved as a result of functional divergence of the ketoreductase LanV and hydroxylase JadH, respectively. Specifically, LanV has acquired affinity for an earlier biosynthetic intermediate resulting in a switch in biosynthetic order and lack of hydroxyls at C-4a and C-12b, whereas in JadH, C-4a/C-12b dehydration has evolved into an independent secondary function replacing C-12b hydroxylation. Importantly, the study reveals that many of the modification enzymes carry several alternative, hidden, or ancestral catalytic functions, which are strictly dependent on the biosynthetic context.

  DOI：

  10.1016/j.chembiol.2012.04.010