1,5,8-[13C]-chorismic acid | 1372785-82-4

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: 1,5,8-[13C]-chorismic acid
• CAS: 1372785-82-4
• 化学式: C₁₀H₁₀O₆
• 分子量: 229.153
• InChiKey: WTFXTQVDAKGDEY-IFAWQWESSA-N

反应信息

• 作为反应物：
  描述：

  1,5,8-[13C]-chorismic acid 在 recombinant Bacillus subtilis chorismate mutase 作用下， 反应 15.0h， 生成 2,4,6-[13C]-prephenic acid
  参考文献：
  名称：

  Olefin Isomerization Regiochemistries during Tandem Action of BacA and BacB on Prephenate in Bacilysin Biosynthesis

  摘要：

  BacA and BacB, the first two enzymes of the bacilysin pathway, convert prephenate to an exocylic regio-isomer of dihydrohydroxyphenylpyruvate (ex-H2HPP) on the way to the epoxycyclohexanone warhead in the dipeptide antibiotic, bacilysin. BacA decarboxylates prephenate without aromatization, converting the 1,4-diene in prephenate to the endocyclic 1,3-diene in Delta(4),Delta(8)-dihydrohydroxyphenylpyruvate (en-H2HPP). BacB then performs an allylic isomerization to bring the diene into conjugation with the 2-ketone in the product Delta(3),Delta(5)-dihydrohydroxyphenylpyruvate (ex-H2HPP). To prove that BacA acts regiospecifically on one of the two prochiral olefins in prephenate, we generated 1,5,8-[C-13]-chorismate from bacterial fermentation of 5-[C-13]-glucose and in turn produced 2,4,6-[C-13]-prephenate via chorismate mutase. Tandem action of BacA and BacB gave 2,4,8-[C-13]-7R-ex-H2HPP, showing that Bath isomerizes only the pro-R double bond in prephenate. Nonenzymatic isomerization of the Bath product into conjugation gives only the Delta E-3-geometric isomer of Delta(3),Delta(5)-ex-H2HPP. On the other hand, acceleration of the allylic isomerization by BacB gives a mixture of the E- and Z-geometric isomers of the 7R- product, indicating some rerouting of the flux, likely through dienolate geometric isomers.

  DOI：

  10.1021/bi300254u
• 作为产物：
  描述：

  D-[5-13C]glucose 在 Aerobacter aerogenes (Klebsiella pneumoniae) 62-1 cell culture 作用下， 反应 15.0h， 以56 mg的产率得到1,5,8-[13C]-chorismic acid
  参考文献：
  名称：

  Olefin Isomerization Regiochemistries during Tandem Action of BacA and BacB on Prephenate in Bacilysin Biosynthesis

  摘要：

  BacA and BacB, the first two enzymes of the bacilysin pathway, convert prephenate to an exocylic regio-isomer of dihydrohydroxyphenylpyruvate (ex-H2HPP) on the way to the epoxycyclohexanone warhead in the dipeptide antibiotic, bacilysin. BacA decarboxylates prephenate without aromatization, converting the 1,4-diene in prephenate to the endocyclic 1,3-diene in Delta(4),Delta(8)-dihydrohydroxyphenylpyruvate (en-H2HPP). BacB then performs an allylic isomerization to bring the diene into conjugation with the 2-ketone in the product Delta(3),Delta(5)-dihydrohydroxyphenylpyruvate (ex-H2HPP). To prove that BacA acts regiospecifically on one of the two prochiral olefins in prephenate, we generated 1,5,8-[C-13]-chorismate from bacterial fermentation of 5-[C-13]-glucose and in turn produced 2,4,6-[C-13]-prephenate via chorismate mutase. Tandem action of BacA and BacB gave 2,4,8-[C-13]-7R-ex-H2HPP, showing that Bath isomerizes only the pro-R double bond in prephenate. Nonenzymatic isomerization of the Bath product into conjugation gives only the Delta E-3-geometric isomer of Delta(3),Delta(5)-ex-H2HPP. On the other hand, acceleration of the allylic isomerization by BacB gives a mixture of the E- and Z-geometric isomers of the 7R- product, indicating some rerouting of the flux, likely through dienolate geometric isomers.

  DOI：

  10.1021/bi300254u