6-endo-hydroxycamphor | 1935-16-6

• 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: 6-endo-hydroxycamphor
• 英文别名: (1S,2R)-1-methyl-2-hydroxy-7,7-dimethyl-bicyclo[2,2,1]hept-6-one；(1S,4R,6R)-(+)-6-endo-hydroxycamphor；(+)-6-Endo-hydroxycamphor；(1S,4R,6R)-6-hydroxy-1,7,7-trimethylbicyclo[2.2.1]heptan-2-one
• CAS: 1935-16-6
• 化学式: C₁₀H₁₆O₂
• 分子量: 168.236
• InChiKey: UNOCSJVDJYDPTN-XSSZXYGBSA-N

物化性质

• 沸点：
  250.9±23.0 °C(Predicted)
• 密度：
  1.107±0.06 g/cm3(Predicted)

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

• 作为反应物：
  描述：

  6-endo-hydroxycamphor 以 氘代氯仿 为溶剂， 生成 6-exo-hydroxycamphor
  参考文献：
  名称：

  Multiple Monohydroxylation Products from rac-Camphor by Marine Fungus Botryosphaeria sp. Isolated from Marine Alga Bostrychia radicans

  摘要：

  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.

  DOI：

  10.21577/0103-5053.20160262
• 作为产物：
  描述：

  epidioxy-2,6 bornane 在 sodium hydroxide 作用下， 生成 6-endo-hydroxycamphor
  参考文献：
  名称：

  Intervention d'un mecanisme ionique dans la photooxygenation sensibilisee de l′α-pinene en milieu protique

  摘要：

  DOI：

  10.1016/s0040-4039(00)93164-2

文献信息

• Methods and systems for evaluating and predicting the reactivity of monooxygenase enzymes
  申请人：Fasan Rudi

  公开号：US09273342B2

  公开（公告）日：2016-03-01

  Methods and systems for evaluating and predicting the reactivity of natural and engineered monooxygenase enzymes are provided. Methods are provided for acquiring a functional profile (fingerprint) of monooxygenases that encode information regarding the active site configuration of such monooxygenases. Methods are also provided for carrying out analysis of a monooxygenase fingerprint, to formulate predictions regarding the reactivity properties (e.g., substrate reactivity, chemo-, regio, and stereoselectivity properties) of the fingerprinted monooxygenases.

  提供了评估和预测天然和工程单加氧酶酶反应性的方法和系统。提供了获取编码有关这些单加氧酶的活性位点配置信息的功能概要（指纹）的方法。还提供了进行单加氧酶指纹分析，以制定关于指纹化单加氧酶的反应性属性（例如底物反应性、化学、区域和立体选择性属性）的预测的方法。
• Exploring the substrate specificity of Cytochrome P450cin
  作者：Jeanette E. Stok、Peter D. Giang、Siew Hoon Wong、James J. De Voss

  DOI：10.1016/j.abb.2019.07.025

  日期：2019.9

  Initial screening indicated that P450cin could catalyse the oxidation of most of the monoterpenes tested; however, sesquiterpenes were not substrates for this enzyme or the N242A mutant. Additionally, both P450cin mutants were found to be able to oxidise other bicyclic monoterpenes. For example, the oxidation of (R)- and (S)-camphor by N242T favoured the production of 5-endo-hydroxycamphor (65-77% of the

  细胞色素P450是催化多种化合物氧化的酶，这些化合物从较小的挥发性化合物（如单萜）到较大的化合物（如类固醇）不等。可以对这些酶进行修饰，以选择性地氧化感兴趣的底物，从而使其在生物技术工业中的应用具有吸引力。在这项研究中，我们筛选了一个针对P450cin和两个P450cin突变体N242A和N242T的萜烯和类萜化合物的小文库，先前已证明它们会影响选择性。初步筛选表明，P450cin可以催化大多数测试的单萜的氧化。然而，倍半萜烯不是该酶或N242A突变体的底物。另外，发现两个P450cin突变体都能够氧化其他双环单萜。例如，N242T对（R）和（S）樟脑的氧化作用有利于生成5-内羟基樟脑（总产物的65-77％，取决于对映异构体），这与以前对（R ）-用N242A（73％）制成的樟脑。还观察到（R）-和（S）-柠檬烯的选择性，其中N242A主要产生顺式-柠檬烯1,2-环氧化物（（R）-柠檬烯氧
• P450 Fingerprinting Method for Rapid Discovery of Terpene Hydroxylating P450 Catalysts with Diversified Regioselectivity
  作者：Kaidong Zhang、Shady El Damaty、Rudi Fasan

  DOI：10.1021/ja109590h

  日期：2011.3.16

  Engineered P450 enzymes constitute attractive catalysts for the selective oxidation of unactivated C-H bonds in complex molecules. A current bottleneck in the use of P450 catalysis for chemical synthesis is the time and effort required to identify the P450 variant(s) with the desired level of activity and selectivity. In this report, we describe a method to map the active site configuration of engineered P450 variants in high throughput using a set of semisynthetic chromogenic probes. Through analysis of the resulting 'fingerprints', reliable predictions can be made regarding the reactivity of these enzymes toward complex substrates structurally related to the fingerprint probes. In addition, fingerprint analysis offers a convenient and time-effective means to assess the regioselectivity properties of the fingerprinted P450s. The described approach can represent a valuable tool to expedite the discovery of P450 oxidation catalysts for the functionalization of relevant natural products such as members of the terpene family.
• 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.
• P450 camr , a cytochrome P450 catalysing the stereospecific 6- endo -hydroxylation of (1 R )-(+)-camphor
  作者：Grogan G.、Roberts G.、Parsons S.、Turner N.、Flitsch S.

  DOI：10.1007/s00253-002-1054-0

  日期：2002.1.1

  Rhodococcus sp. NCIMB 9784 accumulated 6-endo-hydroxycamphor 3 when grown on (1R)-(+)camphor 1 as sole carbon source. The structure of 3 has been unambiguously assigned for the first time using Xray crystallography. A soluble cytochrome P450 hydroxylase, induced by growth on (1R)-(+)-camphor and designated P450(camr), has been isolated from the bacterium Rhodococcus sp. NCIMB 9784. Using authentic 6-endo hydroxycamphor as standard, a cell-free system consisting of pure P450(camr) and putidaredoxin and putidaredoxin reductase from Pseudomonas putida confirmed that the enzyme hydroxylates (1R)-(+)-camphor specifically in the 6-endo position, in contrast to the 5-exo hydroxylation catalysed by the well-studied P450(cam) from P. putida. P450(camr) has a molecular mass of approximately 44 kDa, and a pI of 4.8.