strictosidine aglycone | 85925-13-9

• 分子结构分类: 有机化合物 - 生物碱及其衍生物 - 哈马拉生物碱
• 英文名称: strictosidine aglycone
• 英文别名: methyl (2R,3R,4S)-3-ethenyl-2-hydroxy-4-[[(1S)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-1-yl]methyl]-3,4-dihydro-2H-pyran-5-carboxylate
• CAS: 85925-13-9
• 化学式: C₂₁H₂₄N₂O₄
• 分子量: 368.433
• InChiKey: HXLWDALZXJIPSY-LPIRWUFSSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  27
• 可旋转键数：
  5
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  83.6
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  异胡豆苷 在 Rauvolfia strictosidine O-β-D-glucosidase 作用下， 生成 strictosidine aglycone
  参考文献：
  名称：

  Structures of Alkaloid Biosynthetic Glucosidases Decode Substrate Specificity

  摘要：

  Two similar enzymes with different biosynthetic function in one species have evolved to catalyze two distinct reactions. X-ray structures of both enzymes help reveal their most important differences. The Rauvolfia alkaloid biosynthetic network harbors two O-glucosidases: raucaffricine glucosidase (RG), which hydrolyses raucaffricine to an intermediate downstream in the ajmaline pathway, and strictosidine glucosidase (SG), which operates upstream. RG converts strictosidine, the substrate of SG, but SG does not accept raucaffricine. Now elucidation of crystal structures of RG, inactive RG-E186Q mutant, and its complexes with ligands dihydro-raucaffricine and secologanin reveals that it is the "wider gate" of RG that allows strictosidine to enter the catalytic site, whereas the "slot-like" entrance of SG prohibits access by raucaffricine. Trp392 in RG and Trp388 in SG control the gate shape and acceptance of substrates. Ser390 directs the conformation of Trp392. 3D structures, supported by site-directed mutations and kinetic data of RG and SG, provide a structural and catalytic explanation of substrate specificity and deeper insights into O-glucosidase chemistry.

  DOI：

  10.1021/cb200267w

文献信息

• Compositions and methods for making terpenoid indole alkaloids
  申请人：Willow BioSciences Inc.

  公开号：US11072613B2

  公开（公告）日：2021-07-27

  Methods that may be used for the manufacture of a class of chemical compounds known as terpenoid indole alkaloids, including tabersonine and catharanthine are provided. Compositions useful for the synthesis of terpenoid indole alkaloids, including tabersonine and catharanthine are also provided. The provided compounds are useful in the manufacture of chemotherapeutic agents.

  提供了可用于制造一类称为萜类吲哚生物碱（包括他巴戟碱和卡他蒽碱）的化合物的方法。此外，还提供了用于合成萜类吲哚生物碱（包括他巴戟碱和卡他林碱）的组合物。所提供的化合物可用于制造化疗药物。
• Structures of Alkaloid Biosynthetic Glucosidases Decode Substrate Specificity
  作者：Liqun Xia、Martin Ruppert、Meitian Wang、Santosh Panjikar、Haili Lin、Chitra Rajendran、Leif Barleben、Joachim Stöckigt

  DOI：10.1021/cb200267w

  日期：2012.1.20

  Two similar enzymes with different biosynthetic function in one species have evolved to catalyze two distinct reactions. X-ray structures of both enzymes help reveal their most important differences. The Rauvolfia alkaloid biosynthetic network harbors two O-glucosidases: raucaffricine glucosidase (RG), which hydrolyses raucaffricine to an intermediate downstream in the ajmaline pathway, and strictosidine glucosidase (SG), which operates upstream. RG converts strictosidine, the substrate of SG, but SG does not accept raucaffricine. Now elucidation of crystal structures of RG, inactive RG-E186Q mutant, and its complexes with ligands dihydro-raucaffricine and secologanin reveals that it is the "wider gate" of RG that allows strictosidine to enter the catalytic site, whereas the "slot-like" entrance of SG prohibits access by raucaffricine. Trp392 in RG and Trp388 in SG control the gate shape and acceptance of substrates. Ser390 directs the conformation of Trp392. 3D structures, supported by site-directed mutations and kinetic data of RG and SG, provide a structural and catalytic explanation of substrate specificity and deeper insights into O-glucosidase chemistry.