2-phenyl-N-sulfonatooxyethanimidothioate

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 2-phenyl-N-sulfonatooxyethanimidothioate
• 化学式: C8H7NO4S2-2
• 分子量: 245.3
• InChiKey: HDEIGSIJUBUHSO-UHFFFAOYSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  15
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  88.2
• 氢给体数：
  0
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  2-phenyl-N-sulfonatooxyethanimidothioate 生成 异硫氰酸苯甲酯 、 硫酸酯
  参考文献：
  名称：

  Glucosinolate hydrolysis in Lepidium sativum––identification of the thiocyanate-forming protein

  摘要：

  硫代葡萄糖苷是一类主要存在于十字花科植物中的硫代糖苷，其抗食草动物的作用归因于植物组织受损时由芥子酶催化水解形成的产品。最常见的异硫氰酸盐水解产物对多种生物有毒。根据硫代葡萄糖苷侧链结构和某些蛋白质因子的存在，可以形成其他类型的水解产物，如简单腈、表硫腈和有机硫氰酸盐，其生物学功能尚不明确。在控制硫代葡萄糖苷水解的蛋白质中，只有促进形成简单腈和表硫腈的表硫苷酶蛋白（ESP）在分子水平上得到了确认。我们研究了甘蓝中的硫代葡萄糖苷水解，并鉴定了一种形成硫氰酸盐的蛋白（TFP），该蛋白与已知的ESP具有63-68%的氨基酸序列相似性，与拟南芥中的芥子酶结合蛋白具有高达55%的相似性，但在生物化学上与ESP不同。TFP不仅催化苄基硫代葡萄糖苷形成硫氰酸盐和简单腈，还催化脂肪族硫代葡萄糖苷形成简单腈和表硫腈。对甘蓝自溶产物中硫代葡萄糖苷水解产物

  DOI：

  10.1007/s11103-006-9071-5
• 作为产物：
  描述：

  Benzyl glucosinolate 、 水 生成 2-phenyl-N-sulfonatooxyethanimidothioate 、 D-葡萄糖 、 氢(+1)阳离子
  参考文献：
  名称：

  Nitrile-specifier Proteins Involved in Glucosinolate Hydrolysis in Arabidopsis thaliana

  摘要：

  Glucosinolates are plant secondary metabolites present in Brassicaceae plants such as the model plant Arabidopsis thaliana. Intact glucosinolates are believed to be biologically inactive, whereas degradation products after hydrolysis have multiple roles in growth regulation and defense. The degradation of glucosinolates is catalyzed by thioglucosidases called myrosinases and leads by default to the formation of isothiocyanates. The interaction of a protein called epithiospecifier protein ( ESP) with myrosinase diverts the reaction toward the production of epithionitriles or nitriles depending on the glucosinolate structure. Here we report the identification of a new group of nitrile-specifier proteins (AtNSPs) in A. thaliana able to generate nitriles in conjunction with myrosinase and a more detailed characterization of one member (AtNSP2). Recombinant AtNSP2 expressed in Escherichia coli was used to test its impact on the outcome of glucosinolate hydrolysis using a gas chromatography mass spectrometry approach. AtNSP proteins share 30-45% sequence homology with A. thaliana ESP. Although AtESP and AtNSP proteins can switch myrosinase-catalyzed degradation of 2-propenyl-glucosinolate from isothiocyanate to nitrile, only AtESP generates the corresponding epithionitrile. Using the aromatic benzylglucosinolate, recombinant AtNSP2 is also able to direct product formation to the nitrile. Analysis of glucosinolate hydrolysis profiles of transgenic A. thaliana plants overexpressing AtNSP2 confirms its nitrile-specifier activity in planta. In silico expression analysis reveals distinctive expression patterns of AtNSPs, which supports a biological role for these proteins. In conclusion, we show that AtNSPs belonging to a new family of A. thaliana proteins structurally related to AtESP divert product formation from myrosinase-catalyzed glucosinolate hydrolysis and, thereby, likely affect the biological consequences of glucosinolate degradation. We discuss similarities and properties of AtNSPs and related proteins and the biological implications.

  DOI：

  10.1074/jbc.m807500200

文献信息

• A thiocyanate-forming protein generates multiple products upon allylglucosinolate breakdown in Thlaspi arvense
  作者：Jennifer-C. Kuchernig、Anita Backenköhler、Maike Lübbecke、Meike Burow、Ute Wittstock

  DOI：10.1016/j.phytochem.2011.06.013

  日期：2011.10

  Glucosinolates, amino acid-derived thioglycosides found in plants of the Brassicales order, are one of the best studied classes of plant secondary metabolites. Together with myrosinases and supplementary proteins known as specifier proteins, they form the glucosinolate-myrosinase system that upon tissue damage gives rise to a number of biologically active glucosinolate breakdown products such as isothiocyanates, epithionitriles and organic thiocyanates involved in plant defense. While isothiocyanates are products of the spontaneous rearrangement of the glucosinolate aglycones released by myrosinase, the formation of epithionitriles and organic thiocyanates depends on both myrosinases and specifier proteins. Hydrolysis product profiles of many glucosinolate-containing plant species indicate the presence of specifier proteins, but only few have been identified and characterized biochemically. Here, we report on cDNA cloning, heterologous expression and characterization of TaTFP, a thiocyanate-forming protein (TFP) from Thlaspi arvense L. (Brassicaceae), that is expressed in all plant organs and can be purified in active form after heterologous expression in Escherichia coli. As a special feature, this protein promotes the formation of allylthiocyanate as well as the corresponding epithionitrile upon myrosinase-catalyzed hydrolysis of allylglucosinolate, the major glucosinolate of T. arvense. All other glucosinolates tested are converted to their simple nitriles when hydrolyzed in the presence of TaTFP. Despite its ability to promote allylthiocyanate formation, TaTFP has a higher amino acid sequence similarity to known epithiospecifier proteins (ESPs) than to Lepidium sativum TFP. However, unlike Arabidopsis thaliana ESP, its activity in vitro is not strictly dependent on Fe2+ addition to the assay mixtures. The availability of TaTFP in purified form enables future studies to be aimed at elucidating the structural bases of specifier protein specificities and mechanisms. Furthermore, identification of TaTFP shows that product specificities of specifier proteins can not be predicted based on amino acid sequence similarity and raises interesting questions about specifier protein evolution. (C) 2011 Elsevier Ltd. All rights reserved.
• Nitrile-specifier Proteins Involved in Glucosinolate Hydrolysis in Arabidopsis thaliana
  作者：Ralph Kissen、Atle M. Bones

  DOI：10.1074/jbc.m807500200

  日期：2009.5

  Glucosinolates are plant secondary metabolites present in Brassicaceae plants such as the model plant Arabidopsis thaliana. Intact glucosinolates are believed to be biologically inactive, whereas degradation products after hydrolysis have multiple roles in growth regulation and defense. The degradation of glucosinolates is catalyzed by thioglucosidases called myrosinases and leads by default to the formation of isothiocyanates. The interaction of a protein called epithiospecifier protein ( ESP) with myrosinase diverts the reaction toward the production of epithionitriles or nitriles depending on the glucosinolate structure. Here we report the identification of a new group of nitrile-specifier proteins (AtNSPs) in A. thaliana able to generate nitriles in conjunction with myrosinase and a more detailed characterization of one member (AtNSP2). Recombinant AtNSP2 expressed in Escherichia coli was used to test its impact on the outcome of glucosinolate hydrolysis using a gas chromatography mass spectrometry approach. AtNSP proteins share 30-45% sequence homology with A. thaliana ESP. Although AtESP and AtNSP proteins can switch myrosinase-catalyzed degradation of 2-propenyl-glucosinolate from isothiocyanate to nitrile, only AtESP generates the corresponding epithionitrile. Using the aromatic benzylglucosinolate, recombinant AtNSP2 is also able to direct product formation to the nitrile. Analysis of glucosinolate hydrolysis profiles of transgenic A. thaliana plants overexpressing AtNSP2 confirms its nitrile-specifier activity in planta. In silico expression analysis reveals distinctive expression patterns of AtNSPs, which supports a biological role for these proteins. In conclusion, we show that AtNSPs belonging to a new family of A. thaliana proteins structurally related to AtESP divert product formation from myrosinase-catalyzed glucosinolate hydrolysis and, thereby, likely affect the biological consequences of glucosinolate degradation. We discuss similarities and properties of AtNSPs and related proteins and the biological implications.
• Glucosinolate hydrolysis in Lepidium sativum––identification of the thiocyanate-forming protein
  作者：Meike Burow、Andrea Bergner、Jonathan Gershenzon、Ute Wittstock

  DOI：10.1007/s11103-006-9071-5

  日期：2006.12.7

  Glucosinolates are a class of thioglycosides found predominantly in plants of the order Brassicales whose function in anti-herbivore defense has been attributed to the products formed by myrosinase-catalyzed hydrolysis upon plant tissue damage. The most common type of hydrolysis products, the isothiocyanates, are toxic to a wide range of organisms. Depending on the glucosinolate side-chain structure and the presence of certain protein factors, other types of hydrolysis products, such as simple nitriles, epithionitriles and organic thiocyanates, can be formed whose biological functions are not well understood. Of the proteins controlling glucosinolate hydrolysis, only epithiospecifier proteins (ESPs) that promote the formation of simple nitriles and epithionitriles have been identified on a molecular level. We investigated glucosinolate hydrolysis in Lepidium sativum and identified a thiocyanate-forming protein (TFP) that shares 63-68% amino acid sequence identity with known ESPs and up to 55% identity with myrosinase-binding proteins from Arabidopsis thaliana, but differs from ESPs in its biochemistry. TFP does not only catalyze thiocyanate and simple nitrile formation from benzylglucosinolate but also the formation of simple nitriles and epithionitriles from aliphatic glucosinolates. Analyses of glucosinolate hydrolysis products in L. sativum autolysates and TFP transcript accumulation revealed an organ-specific regulation of thiocyanate formation. The identification of TFP defines a new family of proteins that control glucosinolate hydrolysis and challenges the previously proposed reaction mechanism of epithionitrile formation. As a protein that promotes the formation of a wide variety of hydrolysis products, its identification provides an important tool for further elucidating the mechanisms of glucosinolate hydrolysis as well as the ecological role and the evolutionary origin of the glucosinolate-myrosinase system.

  硫代葡萄糖苷是一类主要存在于十字花科植物中的硫代糖苷，其抗食草动物的作用归因于植物组织受损时由芥子酶催化水解形成的产品。最常见的异硫氰酸盐水解产物对多种生物有毒。根据硫代葡萄糖苷侧链结构和某些蛋白质因子的存在，可以形成其他类型的水解产物，如简单腈、表硫腈和有机硫氰酸盐，其生物学功能尚不明确。在控制硫代葡萄糖苷水解的蛋白质中，只有促进形成简单腈和表硫腈的表硫苷酶蛋白（ESP）在分子水平上得到了确认。我们研究了甘蓝中的硫代葡萄糖苷水解，并鉴定了一种形成硫氰酸盐的蛋白（TFP），该蛋白与已知的ESP具有63-68%的氨基酸序列相似性，与拟南芥中的芥子酶结合蛋白具有高达55%的相似性，但在生物化学上与ESP不同。TFP不仅催化苄基硫代葡萄糖苷形成硫氰酸盐和简单腈，还催化脂肪族硫代葡萄糖苷形成简单腈和表硫腈。对甘蓝自溶产物中硫代葡萄糖苷水解产物