(-)-(1S,4S,5R)-5-endo-hydroxycamphor

• 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: (-)-(1S,4S,5R)-5-endo-hydroxycamphor
• 英文别名: 5-endo-hydroxycamphor；(1S,4S,5R)-5-hydroxy-1,7,7-trimethylbicyclo[2.2.1]heptan-2-one
• 化学式: C₁₀H₁₆O₂
• 分子量: 168.236
• InChiKey: DJQYBVLXBVJHMU-BRDIYROLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1
• 重原子数：
  12
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.9
• 拓扑面积：
  37.3
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  左旋樟脑 在 氧气 作用下， 以89%的产率得到(-)-(1S,4S,5R)-5-endo-hydroxycamphor
  参考文献：
  名称：

  使用P450 SMO还原酶结构域进行电子转移的人工自足P450进行单萜羟基化

  摘要：

  细胞色素P450 SMO从红球菌属。ECU0066是一种天然的自给自足的P450单加氧酶，由血红素结构域，含有FMN和NADPH结合位点的黄素还原酶结构域以及[Fe 2 S 2 ]铁氧还蛋白结构域组成。P450凸轮可将樟脑羟基化为5-exo-hydroxy樟脑。据报道，变体P450 cam（Y96F / V247L）可通过蛋白质工程技术氧化单萜。在这项工作中，我们通过将P450 SMO还原酶结构域和P450 cam（Y96F / V247L）域与一个连接子区域（G 4 S）连接在一起，构建了一个人工自给自足的P450型单萜羟化酶。4。所得的嵌合P450酶可催化（-）-柠檬烯和α- pine烯以及樟脑的羟基化作用，而这些酶对天然融合蛋白P450 SMO均无活性。融合的P450与葡萄糖脱氢酶（GDH）的共表达改善了（-）-柠檬烯的转化率，因为在以葡萄糖为共底物的体系中可以再生出足够的NADPH。这项工作表明，P450

  DOI：

  10.1016/j.molcatb.2015.02.006

文献信息

• In vivo and in vitro hydroxylation of cineole and camphor by cytochromes P450CYP101A1, CYP101B1 and N242A CYP176A1
  作者：Jeanette E. Stok、Emma A. Hall、Isobella S.J. Stone、Margaret C. Noble、Siew Hoon Wong、Stephen G. Bell、James J. De Voss

  DOI：10.1016/j.molcatb.2016.03.004

  日期：2016.6

  Cytochromes P450 (P450s) are valuable enzymes that can generate a range of useful compounds via biocatalytic oxidations that complement traditional synthetic chemistry. In this study three bacterial P450s, qP450(cam) (CYP101A1), CYP101B1 and the mutant N242A-P450(cin) (N242A-CYP176A1), were used to produce a range of products from the oxidation of the monoterpenes (1R)- and (1S) -camphor and 1,8-cineole. We demonstrate that both in vitro and in vivo catalytic turnover with these P450s can produce a complement of up to seven hydroxycamphors and seven hydroxycineoles, in addition to compounds produced from further oxidation. The CYP101B1 whole cell catalytic system was found to produce 300-600 mg/L of culture of oxidation products that could be easily separated chromatographically. The CYP101B1 in vitro oxidation of 1,8-cineole primarily produced (1S)-5 alpha-hydroxycineole, which was 78% of the total product formed. However, the amount of (1S)-5a-hydroxycineole was reduced to 42% of the total products when isolated from the CYP101B1 whole cell system. (1S)-6 alpha-Hydroxycineole (96% ee) could be isolated from a whole cell catalytic turnover of 1,8-cineole by N242A-P450c,n in a yield of 46 mg/L (98% of the total product). However, the amount of product isolated ((1R)-5-endo-hydroxycamphor, 75% of the total products) from the whole cell catalytic oxidation of (1R) -camphor with N242A-P450c,n was much lower (6 mg/L) due to the inefficient use of reducing equivalents (3.5 + 0.5%) for substrate oxidation. These compounds will assist in the identification of specific structures in mechanistic investigations and structure elucidation, but further optimisation is required to generate larger quantities for synthetic applications. (C) 2016 Elsevier B.V. All rights reserved.
• Multiple Monohydroxylation Products from rac-Camphor by Marine Fungus Botryosphaeria sp. Isolated from Marine Alga Bostrychia radicans
  作者：Hugo de Jesus、Alex Jeller、Hosana Debonsi、Péricles Alves、André Porto

  DOI：10.21577/0103-5053.20160262

  日期：——

  This manuscript describes the biooxidation of rac-camphor using whole cells of marine-derived fungus Botryosphaeria sp. CBMAI 1197. The main biotransformation products of this monoterpene were achieved via a hydroxylation reaction and occurred with 5 days of rac-camphor incubation. Products were identified by means of gas chromatography mass spectrometry (GC-MS) and nuclear magnetic resonance (NMR) data. The major hydroxylated products were 6-endo-hydroxycamphor, 6-exo-hydroxycamphor, 5-exo-hydroxycamphor, 5-endo-hydroxycamphor, 3-exo-hydroxycamphor and 8-hydroxycamphor. The 6-exo-hydroxycamphor was obtained through a retro-aldol reaction when 6-endo-hydroxycamphor was maintained in presence of CDCl3; this isomerization was confirmed by H-1 NMR and GC-MS data.
• Monoterpene hydroxylation with an artificial self-sufficient P450 utilizing a P450SMO reductase domain for the electron transfer
  作者：Zheng-Jiao Luan、Yue-Cai Yin、Ai-Tao Li、Hui-Lei Yu、Jian-He Xu

  DOI：10.1016/j.molcatb.2015.02.006

  日期：2015.6

  Rhodococcus sp. ECU0066 is a natural self-sufficient P450 monooxygenase, consisting of a heme domain, a flavin-reductase domain containing FMN and NADPH binding sites, and a [Fe2S2] ferredoxin domain. P450cam catalyzes the hydroxylation of camphor to 5-exo-hydroxycamphor. The variant P450cam (Y96F/V247L) was reported for the oxidation of monoterpene by protein engineering. In this work, we constructed an

  细胞色素P450 SMO从红球菌属。ECU0066是一种天然的自给自足的P450单加氧酶，由血红素结构域，含有FMN和NADPH结合位点的黄素还原酶结构域以及[Fe 2 S 2 ]铁氧还蛋白结构域组成。P450凸轮可将樟脑羟基化为5-exo-hydroxy樟脑。据报道，变体P450 cam（Y96F / V247L）可通过蛋白质工程技术氧化单萜。在这项工作中，我们通过将P450 SMO还原酶结构域和P450 cam（Y96F / V247L）域与一个连接子区域（G 4 S）连接在一起，构建了一个人工自给自足的P450型单萜羟化酶。4。所得的嵌合P450酶可催化（-）-柠檬烯和α- pine烯以及樟脑的羟基化作用，而这些酶对天然融合蛋白P450 SMO均无活性。融合的P450与葡萄糖脱氢酶（GDH）的共表达改善了（-）-柠檬烯的转化率，因为在以葡萄糖为共底物的体系中可以再生出足够的NADPH。这项工作表明，P450