(1S,3R)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (1S,3R)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate
• 英文别名: (1S,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropane-1-carboxylate
• 化学式: C8H9Cl2O2-
• 分子量: 208.06
• InChiKey: LLMLSUSAKZVFOA-UJURSFKZSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  4
• 重原子数：
  12
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  40.1
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  (1S,3R)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate 在 methyl 作用下， 以 磷酸肌酸 为溶剂， 反应 96.0h， 以0.277 g of 2,2-dimethyl-3-(2,2-dichlorovinyl)cyclopropane carboxylic acid was obtained的产率得到二氯菊酸
  参考文献：
  名称：

  Method for producing optically active cyclopropane carboxylic acid

  摘要：

  本发明涉及一种制备光学活性环丙烷羧酸衍生物及其盐的过程，其由式（III）表示：##STR1##其中X是氯原子、溴原子、甲基基团或三氟甲基基团，R'是氢原子或金属离子，通过使用特定菌株或其酯酶不对称水解具有式（II）的环丙烷羧酸酯，其中X如上定义，R是C.sub.1-4烷基或卤代C.sub.1-4烷基。

  公开号：

  US05180671A1
• 作为产物：
  描述：

  trans-permethrin 、 水 生成 (1S,3R)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate 、 3-苯氧基苄醇 、 氢(+1)阳离子
  参考文献：
  名称：

  从克雷伯菌属的新型拟除虫菊酯水解酯酶的分子克隆，纯化和生化特性。菌株ZD112。

  摘要：

  来自克雷伯菌的编码拟除虫菊酯水解酯酶（EstP）的基因。菌株ZD112被克隆到大肠杆菌中并测序。对负责estP基因的DNA进行的序列分析揭示了一个1914 bp的开放阅读框，编码一个637个氨基酸残基的蛋白质。使用酯酶和脂肪酶的核苷酸序列和推导的氨基酸序列，通过数据库同源性搜索未发现相似性。EstP在大肠杆菌中异源表达并纯化。通过凝胶过滤测定，天然酶的分子量约为73kDa。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳的结果和推断的EstP氨基酸序列分别表明分子量为73和73.5 kDa，表明EstP是单体。纯化的EstP不仅降解了许多拟除虫菊酯农药和有机磷杀虫剂马拉硫磷，而且还水解了各种脂肪酸的Rho-硝基苯基酯，这表明EstP是具有广泛底物的酯酶。反式和顺氯菊酯的K（m）值和k（cat）/ K（m）值表明，EstP水解这两种底物的效率均高于抗性昆虫和哺乳动物的羧酸酯酶。Hg2 +，Ag +和rho

  DOI：

  10.1021/jf052691u

文献信息

• Molecular Cloning, Purification, and Biochemical Characterization of a Novel Pyrethroid-Hydrolyzing Esterase from <i>Klebsiella</i> sp. Strain ZD112
  作者：Pei C. Wu、Yu H. Liu、Zhuo Y. Wang、Xiao Y. Zhang、He Li、Wei Q. Liang、Na Luo、Ji M. Hu、Jia Q. Lu、Tian G. Luan、Li X. Cao

  DOI：10.1021/jf052691u

  日期：2006.2.1

  and the organophosphorus insecticide malathion, but also hydrolyzed rho-nitrophenyl esters of various fatty acids, indicating that EstP is an esterase with broad substrates. The K(m) for trans- and cis-permethrin and k(cat)/K(m) values indicate that EstP hydrolyzes both these substrates with higher efficiency than the carboxylesterases from resistant insects and mammals. The catalytic activity of EstP

  来自克雷伯菌的编码拟除虫菊酯水解酯酶（EstP）的基因。菌株ZD112被克隆到大肠杆菌中并测序。对负责estP基因的DNA进行的序列分析揭示了一个1914 bp的开放阅读框，编码一个637个氨基酸残基的蛋白质。使用酯酶和脂肪酶的核苷酸序列和推导的氨基酸序列，通过数据库同源性搜索未发现相似性。EstP在大肠杆菌中异源表达并纯化。通过凝胶过滤测定，天然酶的分子量约为73kDa。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳的结果和推断的EstP氨基酸序列分别表明分子量为73和73.5 kDa，表明EstP是单体。纯化的EstP不仅降解了许多拟除虫菊酯农药和有机磷杀虫剂马拉硫磷，而且还水解了各种脂肪酸的Rho-硝基苯基酯，这表明EstP是具有广泛底物的酯酶。反式和顺氯菊酯的K（m）值和k（cat）/ K（m）值表明，EstP水解这两种底物的效率均高于抗性昆虫和哺乳动物的羧酸酯酶。Hg2 +，Ag +和rho
• Purification and preliminary characterization of permethrinase from a pyrethroid-transforming strain of Bacillus cereus
  作者：S E Maloney、A Maule、A R Smith

  DOI：10.1128/aem.59.7.2007-2013.1993

  日期：1993.7

  Bacillus cereus SM3 was isolated on a mineral salts medium with Tween 80 as the primary carbon source. It was able to hydrolyze second- and third-generation pyrethroids, thereby generating noninsecticidal products. The enzyme responsible for this hydrolytic reaction was named permethrinase for this study. This is the first instance in which pyrethroid detoxification has been achieved with a cell-free microbial enzyme system. Permethrinase was purified by ion-exchange chromatography and gel filtration chromatography. The molecular mass of native permethrinase was 61 +/- 3 kDa, as estimated by Sephadex G-100 gel filtration. This novel microbial esterase seems to be a carboxylesterase. Permethrinase activity had an optimum pH of 7.5 and a temperature optimum of 37 degrees C. No cofactors or coenzymes were required for permethrinase activity. The enzyme may be a serine esterase, as it seems to be sensitive to the organophosphorus compound tetraethylpyrophosphate at concentrations in the micromolar range. Addition of dithiothreitol afforded permethrinase protection against the inhibitory effects of the sulfydryl agents p-chloromercuribenzoate and N-ethylmaleimide. The enzyme was stable over a range of temperatures. Cell extracts of strain SM3 also contained another esterase, which was active towards beta-naphthylacetate, but this enzyme was distinct from permethrinase.

  Bacillus cereus SM3是在以Tween 80为主要碳源的矿盐培养基上分离出来的。它能够水解第二代和第三代拟除虫菊酯，从而产生非杀虫的产物。负责这种水解反应的酶被命名为拟除虫菊酯酶。这是第一次使用无细胞微生物酶系统实现拟除虫菊酯解毒。通过离子交换色谱和凝胶过滤色谱纯化了拟除虫菊酯酶。通过Sephadex G-100凝胶过滤估算，原生拟除虫菊酯酶的分子量为61+/-3 kDa。这种新型微生物酯酶似乎是一种羧酸酯酶。拟除虫菊酯酶活性的最适pH为7.5，最适温度为37℃。拟除虫菊酯酶活性不需要辅因子或辅酶。该酶可能是一种丝氨酸酯酶，因为它似乎对微摩尔浓度的有机磷化合物四乙基焦磷酸盐敏感。加入二硫苏糖醇可使拟除虫菊酯酶免受硫醇试剂对其的抑制作用。该酶在一定温度范围内稳定。菌株SM3的细胞提取物还含有另一种酯酶，对β-萘乙酸酯活性，但这种酶与拟除虫菊酯酶不同。
• Purification and Characterization of a Novel Pyrethroid Hydrolase from<i> Aspergillus niger</i> ZD11
  作者：Wei Q. Liang、Zhuo Y. Wang、He Li、Pei C. Wu、Ji M. Hu、Na Luo、Li X. Cao、Yu H. Liu

  DOI：10.1021/jf051460k

  日期：2005.9.1

  The pyrethroid pesticides residues on foods and environmental contamination are a public safety concern. Pretreatment with pyrethroid hydrolase has the potential to alleviate the conditions. For this purpose, a fungus capable of using pyrethroid pesticides as a sole carbon source was isolated from the soil and characterized as Aspergillus nigerZD11. A novel pyrethroid hydrolase from cell extract was purified 41.5-fold to apparent homogeneity with 12.6% overall recovery. It is a monomeric structure with a molecular mass of 56 kDa, a pl of 5.4, and the enzyme activity was optimal at 45 degrees C and pH 6.5. The activities were strongly inhibited by Hg2+, Ag+, and p-chloromercuribenzoate, whereas less pronounced effects (5-10% inhibition) were observed in the presence of the remaining divalent cations, the chelating agent EDTA and phenanthroline. The purified enzyme hydrolyzed various insecticides with similar carboxylester. trans-Permethrin is the preferred substrate.
• Tandem Aldol−Allylation and Aldol−Aldol Reactions with Ketone-Derived Enolsilanes:  Highly Diastereoselective Single-Step Synthesis of Complex Tertiary Carbinols
  作者：Xiaolun Wang、Qinglin Meng、Nicholas R. Perl、Yue Xu、James L. Leighton

  DOI：10.1021/ja053593s

  日期：2005.9.1

  A new tandem aldol-allylation reaction employing ketone-derived enolates has been developed that leads to the rapid, diastereoselective synthesis of tertiary carbinol containing fragments with relevance to polyketide natural product synthesis. In addition, the use of ketone-derived enolates has led to the development of a new tandem aldol-aldol reaction.
• Identification, Expression, and Purification of a Pyrethroidhydrolyzing Carboxylesterase from Mouse Liver Microsomes
  作者：Jeanette E. Stok、Huazhang Huang、Paul D. Jones、Craig E. Wheelock、Christophe Morisseau、Bruce D. Hammock

  DOI：10.1074/jbc.m403673200

  日期：2004.7

  Carboxylesterases are enzymes that catalyze the hydrolysis of a wide range of ester-containing endogenous and xenobiotic compounds. Although the use of pyrethroids is increasing, the specific enzymes involved in the hydrolysis of these insecticides have yet to be identified. A pyrethroid-hydrolyzing enzyme was partially purified from mouse liver microsomes using a fluorescent reporter similar in structure to cypermethrin (Shan, G., and Hammock, B. D. ( 2001) Anal. Biochem. 299, 54 - 62 and Wheelock, C. E., Wheelock, A. M., Zhang, R., Stok, J. E., Morisseau, C., Le Valley, S. E., Green, C. E., and Hammock, B. D. ( 2003) Anal. Biochem. 315, 208 - 222) and subsequently identified as a carboxylesterase (NCBI accession number BAC36707). The expressed sequence tag was then cloned, expressed in baculovirus, and purified to homogeneity. Kinetic constants for a large number of both type I and type II pyrethroid or pyrethroid-like substrates were determined. This esterase possesses similar kinetic constants for cypermethrin and its fluorescent-surrogate (k(cat) = 0.12 +/- 0.03 versus 0.11 +/- 0.01 s(-1)). Compared with their cis-counterparts, trans-permethrin and cypermethrin were hydrolyzed 22- and 4-fold faster, respectively. Of the four fenvalerate isomers the (2R)(alphaR)-isomer was hydrolyzed at least 1 order of magnitude faster than any other isomer. However, it is unlikely that this enzyme accounts for the total pyrethroid hydrolysis in the microsomes because both isoelectrofocusing and native PAGE indicate the presence of a second region of cypermethrin-metabolizing enzymes. A second carboxylesterase gene ( NCBI accession number NM_ 133960), isolated during a cDNA mouse liver library screening, was also found to hydrolyze pyrethroids. Both these enzymes could be used as preliminary tools in establishing the relative toxicity of new pyrethroids.