11-methoxyvinorine

• 分子结构分类: 有机化合物 - 生物碱及其衍生物 - 可吗灵-沙巴秦生物碱
• 英文名称: 11-methoxyvinorine
• 化学式: C₂₂H₂₄N₂O₃
• 分子量: 364.444
• InChiKey: CJRRQMKNRICNIF-NKLRCLOISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.0
• 重原子数：
  27.0
• 可旋转键数：
  2.0
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.55
• 拓扑面积：
  51.13
• 氢给体数：
  0.0
• 氢受体数：
  5.0

反应信息

• 作为产物：
  描述：

  乙酰辅酶A 、 gardneral 在 potassium phosphate 、 recombinant vinorine synthase 作用下， 以 水 为溶剂， 反应 0.5h， 生成 11-methoxyvinorine
  参考文献：
  名称：

  Acetyltransfer in natural product biosynthesis––functional cloning and molecular analysis of vinorine synthase

  摘要：

  Vinorine synthase (EC 2.3.1.160) catalyses the acetyl-CoA- or CoA-dependent reversible formation of the alkaloids vinorine (or 11-methoxy-vinorine) and 16-epi-vellosimine (or gardneral). The forward reaction leads to vinorine, which is a direct biosynthetic precursor along the complex pathway to the monoterpenoid indole alkaloid ajmaline, an antiarrhythmic drug from the Indian medicinal plant Rauvolfia serpentina. Based on partial peptide sequences a cDNA clone was isolated and functionally expressed in Escherichia coli. The K-m values of the native enzyme for gardneral and acetyl-CoA were determined to be 7.5 and 57 muM. The amino acid sequence of vinorine synthase has highest level of identity (28-31%) to that of Papaver salutaridinol acetyltransferase. Fragaria alcohol acyltransferase, and Catharanthus deacetylvindoline acetyltransferase involved in morphine, flavor, and vindoline biosynthesis, respectively. Vinorine synthase is a novel member of the BAHD superfamily of acyltransferases. Site-directed mutagenesis of 13 amino acid residues provided clear evidence that both, His160 and Asp164 of the consensus sequence HxxxD belong to the catalytic center. The Mutations also showed that an amino acid triad is not characteristic of vinorine synthase. The experiments demonstrated the importance of the conserved motif SxL/I/VD near the N-terminus and the consensus sequence DFGWG near the C-terminal. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2004.02.029

文献信息

• Acetyltransfer in natural product biosynthesis––functional cloning and molecular analysis of vinorine synthase
  作者：Anja Bayer、Xueyan Ma、Joachim Stöckigt

  DOI：10.1016/j.bmc.2004.02.029

  日期：2004.5

  Vinorine synthase (EC 2.3.1.160) catalyses the acetyl-CoA- or CoA-dependent reversible formation of the alkaloids vinorine (or 11-methoxy-vinorine) and 16-epi-vellosimine (or gardneral). The forward reaction leads to vinorine, which is a direct biosynthetic precursor along the complex pathway to the monoterpenoid indole alkaloid ajmaline, an antiarrhythmic drug from the Indian medicinal plant Rauvolfia serpentina. Based on partial peptide sequences a cDNA clone was isolated and functionally expressed in Escherichia coli. The K-m values of the native enzyme for gardneral and acetyl-CoA were determined to be 7.5 and 57 muM. The amino acid sequence of vinorine synthase has highest level of identity (28-31%) to that of Papaver salutaridinol acetyltransferase. Fragaria alcohol acyltransferase, and Catharanthus deacetylvindoline acetyltransferase involved in morphine, flavor, and vindoline biosynthesis, respectively. Vinorine synthase is a novel member of the BAHD superfamily of acyltransferases. Site-directed mutagenesis of 13 amino acid residues provided clear evidence that both, His160 and Asp164 of the consensus sequence HxxxD belong to the catalytic center. The Mutations also showed that an amino acid triad is not characteristic of vinorine synthase. The experiments demonstrated the importance of the conserved motif SxL/I/VD near the N-terminus and the consensus sequence DFGWG near the C-terminal. (C) 2004 Elsevier Ltd. All rights reserved.