seco-7-dihydro-10-deoxymethynolide | 872048-01-6

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: seco-7-dihydro-10-deoxymethynolide
• 英文别名: (2R,3S,4S,6R,7R/S,10R,11R,8E)-3,7,11-Trihydroxy-2,4,6,10-tetramethyltridec-8-enoic acid；(E,2R,3S,4S,6R,10R,11R)-3,7,11-trihydroxy-2,4,6,10-tetramethyltridec-8-enoic acid
• CAS: 872048-01-6
• 化学式: C₁₇H₃₂O₅
• 分子量: 316.438
• InChiKey: MJTFLRYPKDUSKE-SHTVOURUSA-N

物化性质

• 沸点：
  512.2±50.0 °C(Predicted)
• 密度：
  1.081±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  22
• 可旋转键数：
  10
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.82
• 拓扑面积：
  98
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  seco-7-dihydro-10-deoxymethynolide 在 manganese(IV) oxide 、 叠氮磷酸二苯酯 、 三乙胺 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 41.0h， 生成 (2R,3S,4S,6R,7R/S,8E,10R,11R)-S-2-acetamidoethyl-3,11-dihydroxy-2,4,6,10-tetramethyl-7-oxotridec-8-enethioate
  参考文献：
  名称：

  Macrolactonization to 10-deoxymethynolide catalyzed by the recombinant thioesterase of the picromycin/methymycin polyketide synthase

  摘要：

  The recombinant thioesterase (TE) domain of the picromycin/methymycin synthase (PICS) catalyzes the macrolactonization of 3, the N-acetylcysteamine thioester of seco-10-deoxymethynolide to generate 10-deoxymethynolide (1) with high efficiency. By contrast, 4, the 7-dihydro derivative of seco-thioester 3, undergoes exclusive hydrolysis by PICS TE to seco-acid 5. The recombinant TE domain of 6-deoxyerythronolide B synthase (DEBS TE) shows the same reaction specificity as PICS TE, but with significantly lower activity. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2005.09.077
• 作为产物：
  描述：

  10-去氧微甘菊内酯 在 lithium hydroxide 、 sodium tetrahydroborate 、 cerium(III) chloride 作用下， 以 甲醇 为溶剂， 反应 55.17h， 生成 seco-7-dihydro-10-deoxymethynolide
  参考文献：
  名称：

  Macrolactonization to 10-deoxymethynolide catalyzed by the recombinant thioesterase of the picromycin/methymycin polyketide synthase

  摘要：

  The recombinant thioesterase (TE) domain of the picromycin/methymycin synthase (PICS) catalyzes the macrolactonization of 3, the N-acetylcysteamine thioester of seco-10-deoxymethynolide to generate 10-deoxymethynolide (1) with high efficiency. By contrast, 4, the 7-dihydro derivative of seco-thioester 3, undergoes exclusive hydrolysis by PICS TE to seco-acid 5. The recombinant TE domain of 6-deoxyerythronolide B synthase (DEBS TE) shows the same reaction specificity as PICS TE, but with significantly lower activity. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2005.09.077

文献信息

• Frontiers and Opportunities in Chemoenzymatic Synthesis
  作者：Jonathan D. Mortison、David H. Sherman

  DOI：10.1021/jo101124n

  日期：2010.11.5

  Natural product biosynthetic pathways have evolved enzymes with myriad activities that represent an expansive array of chemical transformations for constructing secondary metabolites. Recently, harnessing the biosynthetic potential of these enzymes through chemoenzymatic synthesis has provided a powerful tool that often rivals the most sophisticated methodologies in modern synthetic chemistry and provides new opportunities for accessing chemical diversity. Herein, we describe our research efforts with enzymes from a broad collection of biosynthetic systems, highlighting recent progress in this exciting field.
• Chain Elongation, Macrolactonization, and Hydrolysis of Natural and Reduced Hexaketide Substrates by the Picromycin/Methymycin Polyketide Synthase
  作者：Jiaquan Wu、Weiguo He、Chaitan Khosla、David E. Cane

  DOI：10.1002/anie.200502246

  日期：2005.11.25
• Macrolactonization to 10-deoxymethynolide catalyzed by the recombinant thioesterase of the picromycin/methymycin polyketide synthase
  作者：Weiguo He、Jiaquan Wu、Chaitan Khosla、David E. Cane

  DOI：10.1016/j.bmcl.2005.09.077

  日期：2006.1

  The recombinant thioesterase (TE) domain of the picromycin/methymycin synthase (PICS) catalyzes the macrolactonization of 3, the N-acetylcysteamine thioester of seco-10-deoxymethynolide to generate 10-deoxymethynolide (1) with high efficiency. By contrast, 4, the 7-dihydro derivative of seco-thioester 3, undergoes exclusive hydrolysis by PICS TE to seco-acid 5. The recombinant TE domain of 6-deoxyerythronolide B synthase (DEBS TE) shows the same reaction specificity as PICS TE, but with significantly lower activity. (c) 2005 Elsevier Ltd. All rights reserved.