6-(1-methyl-2-oxopropyl)-2,2,5-trimethyl-4H-1,3-dioxin-4-one | 922172-14-3

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 6-(1-methyl-2-oxopropyl)-2,2,5-trimethyl-4H-1,3-dioxin-4-one
• 英文别名: 2,2,5-Trimethyl-6-(3-oxobutan-2-yl)-2H,4H-1,3-dioxin-4-one；2,2,5-trimethyl-6-(3-oxobutan-2-yl)-1,3-dioxin-4-one
• CAS: 922172-14-3
• 化学式: C₁₁H₁₆O₄
• 分子量: 212.246
• InChiKey: CQQMSLLSEFJBLK-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  15
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.64
• 拓扑面积：
  52.6
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  6-(1-methyl-2-oxopropyl)-2,2,5-trimethyl-4H-1,3-dioxin-4-one 在 4-二甲氨基吡啶 、 sodium methylate 、 potassium carbonate 、 三乙胺 、 lithium hexamethyldisilazane 作用下， 以 四氢呋喃 、 甲醇 、 二氯甲烷 为溶剂， 反应 5.0h， 生成 2-methoxy-3,5-dimethyl-6-[(E)-3-methylundec-2-enyl]-4H-pyran-4-one
  参考文献：
  名称：

  Total Synthesis and Biological Evaluation of Verticipyrone and Analogues

  摘要：

  Total synthesis of verticipyrone, a novel NADH-fumarate reductase inhibitor, has been accomplished by a convergent approach using novel "Reverse Julia olefination" method. During total synthetic studies, we also prepared and evaluated several synthetic verticipyrone analogues, some of which exhibited more potent antiparasitic activity than the natural verticipyrone.

  DOI：

  10.1021/ol0626140
• 作为产物：
  描述：

  6-(3-Hydroxybutan-2-yl)-2,2,5-trimethyl-2H,4H-1,3-dioxin-4-one 在 草酰氯 、 二甲基亚砜 、 三乙胺 作用下， 以 二氯甲烷 为溶剂， 以4.00 g的产率得到6-(1-methyl-2-oxopropyl)-2,2,5-trimethyl-4H-1,3-dioxin-4-one
  参考文献：
  名称：

  Total Synthesis and Biological Evaluation of Verticipyrone and Analogues

  摘要：

  Total synthesis of verticipyrone, a novel NADH-fumarate reductase inhibitor, has been accomplished by a convergent approach using novel "Reverse Julia olefination" method. During total synthetic studies, we also prepared and evaluated several synthetic verticipyrone analogues, some of which exhibited more potent antiparasitic activity than the natural verticipyrone.

  DOI：

  10.1021/ol0626140

文献信息

• Mechanism and Stereospecificity of a Fully Saturating Polyketide Synthase Module: Nanchangmycin Synthase Module 2 and Its Dehydratase Domain
  作者：Xun Guo、Tiangang Liu、Chiara R. Valenzano、Zixin Deng、David E. Cane

  DOI：10.1021/ja1073432

  日期：2010.10.27

  Recombinant nanchangmycin synthase module 2 (NANS module 2), with the thioesterase domain from the 6-deoxyerythronolide B synthase (DEBS TE) appended to the C-terminus, was cloned and expressed in Escherichia coli. Incubation of NANS module 2+TE with (+/-)-2-methyl-3-keto-butyryl-N-acetylcysteamine thioester (1), the SNAC analog of the natural ACP-bound substrate, with methylmalonyl-CoA (MM-CoA) in the absence of NADPH gave 3,5,6-trimethy1-4-hydroxypyrone (2), identified by direct comparison with synthetic 2 by radio-TLC-phosphorimaging and LC-ESI(+)-MS-MS. The reaction showed K(cat) 0.5 +/- 0.1 min(-1) and K(m)(1) 19 +/- 5 mM at 0.5 mM MM-CoA and k(cat)(app) 0.26 +/- 0.02 min(-1) and K(m)(MM-CoA) 0.11 +/- 0.02 mM at 8 mM 1. Incubation in the presence of NADPH generated the fully saturated triketide chain elongation product as a 5:3 mixture of (2S,4R)-2,4-dimethy1-5-ketohexanoic acid (3a) and the diastereomeric (2S, 4S)-3b. The structure and stereochemistry of each product was established by comparison with synthetic 3a and 3b by a combination of radio-TLC-phosphorimaging and LC-ESI(-)-MS-MS, as well as chiral capillary GC-MS analysis of the corresponding methyl esters 3a-Me and 3b-Me. The recombinant dehydratase domain from NANS module 2, NANS DH2, was shown to catalyze the formation of an (E)-double bond by syndehydration of the ACP-bound substrate anti-(2R,3R,4S,5R)-2,4-dimethyl-3,5-dihydroxyheptanoyl-ACP6 (4), generated in situ by incubation of (2S,3R)-2-methyl-3-hydroxypentanoyl-SNAC (5), methylmalonyl-CoA, and NADPH with the recombinant [KS6][AT6] didomain and ACP6 from DEBS module 6 along with the ketoreductase from the tylactone synthase module 1 (TYLS KR1). These results also indirectly establish the stereochemistry of the reactions catalyzed by the KR and enoylreductase (ER) domains of NANS module 2.