| 1246637-15-9

• 分子结构分类: 有机化合物 - 有机氧化合物
• CAS: 1246637-15-9
• 化学式: C₂₉H₃₂N₂O₆
• 分子量: 504.583
• InChiKey: WPLHKRAJCLUNRB-BVTXZHOWSA-N

反应信息

• 作为反应物：
  描述：

  在 flavin-dependent-4-hydroxyprotoasukamycin epoxidase AsuE₃, 41 kDa 、 2,6-蒽二酚 、 还原型辅酶Ⅰ 作用下， 以 aq. phosphate buffer 为溶剂， 生成 (2E,4E,6E)-8-Methyl-deca-2,4,6-trienoic acid {(1S,5S,6R)-5-hydroxy-5-[(1E,3E,5E)-6-(2-hydroxy-5-oxo-cyclopent-1-enylcarbamoyl)-hexa-1,3,5-trienyl]-2-oxo-7-oxa-bicyclo[4.1.0]hept-3-en-3-yl}-amide
  参考文献：
  名称：

  Tandem Enzymatic Oxygenations in Biosynthesis of Epoxyquinone Pharmacophore of Manumycin-type Metabolites

  摘要：

  Many natural products contain epoxyquinone pharmacophore with unknown biosynthetic mechanisms. Recent genetic analysis of the asukamycin biosynthetic gene cluster proposed enzyme candidates related to epoxyquinone formation for manumycin-type metabolites. Our biochemical studies reveal that 3-amino-4-hydroxyl benzoic acid (3,4-AHBA) precursor is activated and loaded on aryl carrier protein (AsuC12) by ATP-dependent adenylase (AsuA2). AsuE1 and AsuE3, both single-component flavin-dependent monooxygenases, catalyze the exquisite regio- and enantiospecific postpolyketide synthase (PKS) assembly oxygenations. AsuE1 installs a hydroxyl group on the 3,4-AHB ring to form a 4-hydroxyquinone moiety, which is epoxidized by AsuE3 to yield the epoxyquinone functionality. Despite being a single-component monooxygenase, AsuE1 activity is elicited by AsuE2, a pathway-specific flavin reductase. We further demonstrate that the epoxyquinone moiety is critical for anti-MRSA activity by analyzing the bioactivity of various manumycin-type metabolites produced through mutasynthesis.

  DOI：

  10.1016/j.chembiol.2013.05.006
• 作为产物：
  描述：

  在 single-component flavin-dependent monooxygenase AsuE₁, 43 kDa 、 腺嘌呤黄素 、 还原型辅酶Ⅰ 作用下， 以 aq. phosphate buffer 为溶剂， 生成
  参考文献：
  名称：

  Tandem Enzymatic Oxygenations in Biosynthesis of Epoxyquinone Pharmacophore of Manumycin-type Metabolites

  摘要：

  Many natural products contain epoxyquinone pharmacophore with unknown biosynthetic mechanisms. Recent genetic analysis of the asukamycin biosynthetic gene cluster proposed enzyme candidates related to epoxyquinone formation for manumycin-type metabolites. Our biochemical studies reveal that 3-amino-4-hydroxyl benzoic acid (3,4-AHBA) precursor is activated and loaded on aryl carrier protein (AsuC12) by ATP-dependent adenylase (AsuA2). AsuE1 and AsuE3, both single-component flavin-dependent monooxygenases, catalyze the exquisite regio- and enantiospecific postpolyketide synthase (PKS) assembly oxygenations. AsuE1 installs a hydroxyl group on the 3,4-AHB ring to form a 4-hydroxyquinone moiety, which is epoxidized by AsuE3 to yield the epoxyquinone functionality. Despite being a single-component monooxygenase, AsuE1 activity is elicited by AsuE2, a pathway-specific flavin reductase. We further demonstrate that the epoxyquinone moiety is critical for anti-MRSA activity by analyzing the bioactivity of various manumycin-type metabolites produced through mutasynthesis.

  DOI：

  10.1016/j.chembiol.2013.05.006