5α-孕烷-3α,17α,20β-三醇 | 13933-75-0

• 物质功能分类: 分析化学 - 标准品 - 分析标准品
• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 类固醇和类固醇衍生物
• 中文名称: 5α-孕烷-3α,17α,20β-三醇
• 中文别名: 3-Alpha,17-alpha,20-beta-三羟基-5-alpha-孕烷
• 英文名称: 5α-pregnane-3α,20α-diol
• 英文别名: 5α-pregnane-3α,17,20β_F-triol；5α-Pregnan-3α,17,20β_F-triol；(20R)-5alpha-Pregnane-3alpha,17,20-triol；(3R,5S,8R,9S,10S,13S,14S,17R)-17-[(1R)-1-hydroxyethyl]-10,13-dimethyl-1,2,3,4,5,6,7,8,9,11,12,14,15,16-tetradecahydrocyclopenta[a]phenanthrene-3,17-diol
• CAS: 13933-75-0
• 化学式: C₂₁H₃₆O₃
• 分子量: 336.515
• InChiKey: SCPADBBISMMJAW-MUHHAPIYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.8
• 重原子数：
  24
• 可旋转键数：
  1
• 环数：
  4.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  60.7
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  5α-孕烷-3α,17α,20β-三醇 在 human 20α-hydroxysteroid dehydrogenase (AKR1C1) mutant enzyme Leu308Val 、 烟酰胺腺嘌呤双核苷酸磷酸盐 作用下， 生成 5alpha-孕甾-3alpha-醇-20-酮
  参考文献：
  名称：

  Factorizing the role of a critical leucine residue in the binding of substrate to human 20α-hydroxysteroid dehydrogenase (AKR1C1): Molecular modeling and kinetic studies of the Leu308Val mutant enzyme

  摘要：

  A comparison of the structures and kinetic properties of human 20 alpha-hydroxysteroid dehydrogenase (AKR1C1) and its mutant enzymes (Leu308Val and Leu308Ala) indicates that Leu308 is a selectivity determinant for substrate binding. While the Leu308Val mutation improved the catalytic efficiency (k(cat)/K(m)) of AKR1C1 towards the two substrates 5 alpha-pregnane-3 alpha,20a-diol (PregA) and 5 beta-pregnan-3 alpha-ol-20-one (PregB), the Leu308Ala mutation rendered the enzyme inactive. In the docked model of PregA the conformation of the steroid molecule was similar to that of 20 alpha-hydroxyprogesterone in the crystal structure of the AKR1C1 complex where the steroid did not interact with the catalytic residues Tyr55 and His117. In the case of PregB the steroid interacted with the catalytic residue His117 and formed close contacts with Leu308, suggesting that the binding mechanism of 3 alpha-hydroxysteroids in the active site of AKR1C1 is different from that of 20 alpha-hydroxysteroids. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2010.06.137
• 作为产物：
  描述：

  5-Alpha-妊娠-3-alpha-17-二醇-20-酮 在 甲醇 、 sodium tetrahydroborate 作用下， 生成 5α-孕烷-3α,17α,20β-三醇
  参考文献：
  名称：

  Synthesis of 17α,20α-Dihydroxysteroids¹

  摘要：

  DOI：

  10.1021/jo01096a006

文献信息

• METHODS, COMPOSITIONS, AND KITS FOR THE TREATMENT OF CANCER
  申请人：Haggerty Timothy J.

  公开号：US20140335050A1

  公开（公告）日：2014-11-13

  The invention features methods, compositions, and kits for the administration of an HSP90 inhibitor, OBAA, flunarizine, aphidicolin, damnacanthal, dantrolene, or an analog thereof, alone, or in combination with, e.g., a TAA, an antigen-binding scaffold (e.g., an antibody, a soluble T cell receptor, or a chimeric receptor) specific for a TAA, a cell (e.g., a white blood cell that targets a cancer cell), and/or an IFN-β receptor agonist or an IFN-γ receptor agonist, for the treatment of cancer.
• Factorizing the role of a critical leucine residue in the binding of substrate to human 20α-hydroxysteroid dehydrogenase (AKR1C1): Molecular modeling and kinetic studies of the Leu308Val mutant enzyme
  作者：Urmi Dhagat、Satoshi Endo、Midori Soda、Akira Hara、Ossama El-Kabbani

  DOI：10.1016/j.bmcl.2010.06.137

  日期：2010.9

  A comparison of the structures and kinetic properties of human 20 alpha-hydroxysteroid dehydrogenase (AKR1C1) and its mutant enzymes (Leu308Val and Leu308Ala) indicates that Leu308 is a selectivity determinant for substrate binding. While the Leu308Val mutation improved the catalytic efficiency (k(cat)/K(m)) of AKR1C1 towards the two substrates 5 alpha-pregnane-3 alpha,20a-diol (PregA) and 5 beta-pregnan-3 alpha-ol-20-one (PregB), the Leu308Ala mutation rendered the enzyme inactive. In the docked model of PregA the conformation of the steroid molecule was similar to that of 20 alpha-hydroxyprogesterone in the crystal structure of the AKR1C1 complex where the steroid did not interact with the catalytic residues Tyr55 and His117. In the case of PregB the steroid interacted with the catalytic residue His117 and formed close contacts with Leu308, suggesting that the binding mechanism of 3 alpha-hydroxysteroids in the active site of AKR1C1 is different from that of 20 alpha-hydroxysteroids. (C) 2010 Elsevier Ltd. All rights reserved.
• Synthesis of 17α,20α-Dihydroxysteroids¹
  作者：DAVID K. FUKUSHIMA、EVELYN D. MEYER

  DOI：10.1021/jo01096a006

  日期：1958.2