benzyl desulphoglucosinolate | 5115-74-2

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: benzyl desulphoglucosinolate
• 英文别名: desulfobenzylglucosinolate；desulphoglucotropaeolin；desulfoglucotropaeolin；S-(2-Phenyl-acetohydroximoyl)-1-thio-β-D-glucopyranose；1-S-(N-hydroxy-2-phenylethanimidoyl)-1-thio-beta-D-glucopyranose；[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl] N-hydroxy-2-phenylethanimidothioate
• CAS: 5115-74-2
• 化学式: C₁₄H₁₉NO₆S
• 分子量: 329.374
• InChiKey: QXWFHEDNDCNERW-LPUQOGTASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.4
• 重原子数：
  22
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  148
• 氢给体数：
  5
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  PAPS 、 benzyl desulphoglucosinolate 生成 Adenosine 3',5'-bismonophosphate(4-) 、 Benzyl glucosinolate 、 氢(+1)阳离子
  参考文献：
  名称：

  芸苔属物种中催化芥子油苷生物合成的糖基化和硫酸化步骤的酶的放射测定。

  摘要：

  设计了一种测定尿苷二磷酸葡萄糖（UDPglucose）：硫代氢氧肟酸葡萄糖基转移酶和3'-磷酸腺苷-5'-磷酸硫酸盐：脱硫葡萄糖苷磺酸磺基转移酶的新方法。该测定系统基于通过差异吸附到DEAE离子交换盘上分别从阴离子[14C] UDP葡萄糖和阴离子[14C]苄基葡萄糖苷中分离出非离子[14C]去磺基苄基芥子油酸酯。该程序消除了复杂的色谱技术。该方法用于测量几种芸苔属植物中的两种酶。另外，在从甘蓝型油菜（cv Westar）的幼苗的部分纯化期间监测磺基转移酶活性。

  DOI：

  10.1016/0003-2697(89)90369-2
• 作为产物：
  描述：

  苯乙醛肟 在 N-氯代丁二酰亚胺 、 sodiumsulfide nonahydrate 、 DL-dithiothreitol 、 calf intestine alkaline phosphatase 、 UDP-glycosyltransferase 74B₁ from Arabidopsis thaliana 、 三乙胺 作用下， 以 aq. phosphate buffer 、 乙醚 、 水 、 二甲基亚砜 、 N,N-二甲基甲酰胺 为溶剂， 反应 16.5h， 生成 benzyl desulphoglucosinolate
  参考文献：
  名称：

  来自拟南芥的UGT74B1作为通用的生物催化剂，用于合成硫代硫代葡萄糖苷†

  摘要：

  硫糖苷，即使在自然界中很少见，也因其生物学特性而受到越来越多的关注。这类化合物的化学合成已被广泛研究，但有关其生物合成的报道却很少。在此，我们结合酶学，生物有机化学和分子建模等不同领域的实验，希望证明葡糖基转移酶UGT74B1的多功能性及其合成能力，可用于制备多种天然和非天然的脱硫糖基磺酸盐。

  DOI：

  10.1039/c6ob01003b

文献信息

• FIRST SYNTHESIS OF A MUSTARD OIL GLUCOSIDE; THE ENZYMATIC LOSSEN REARRANGEMENT
  作者：Martin G. Ettlinger、Allan J. Lundeen

  DOI：10.1021/ja01564a066

  日期：1957.4
• Metabolite profiling of Arabidopsis seedlings in response to exogenous sinalbin and sulfur deficiency
  作者：Jixiu Zhang、Xiumei Sun、Zhiping Zhang、Yuwen Ni、Qing Zhang、Xinmiao Liang、Hongbin Xiao、Jiping Chen、James G. Tokuhisa

  DOI：10.1016/j.phytochem.2011.06.002

  日期：2011.10

  In order to determine how plant uptake of a sulfur-rich secondary metabolite, sinalbin, affects the metabolic profile of sulfur-deficient plants, gas chromatography time-of-flight mass spectrometry (GC-TOF-MS), in combination with liquid chromatography-mass spectrometry (LC-MS), was used to survey the metabolome of Arabidopsis seedlings grown in nutrient media under different sulfur conditions. The growth media had either sufficient inorganic sulfur for normal plant growth or insufficient inorganic sulfur in the presence or absence of supplementation with organic sulfur in the form of sinalbin (p-hydroxybenzylglucosinolate). A total of 90 metabolites were identified by GC-TOF-MS and their levels were compared across the three treatments. Of the identified compounds, 21 showed similar responses in plants that were either sulfur deficient or sinalbin supplemented compared to sulfur-sufficient plants, while 12 metabolites differed in abundance only in sulfur-deficient plants. Twelve metabolites accumulated to higher levels in sinalbin-supplemented than in the sulfur-sufficient plants. Secondary metabolites such as flavonol conjugates, sinapinic acid esters and glucosinolates, were identified by LC-MS and their corresponding mass fragmentation patterns were determined. Under sinalbin-supplemented conditions, sinalbin was taken up by Arabidopsis and contributed to the endogenous formation of glucosinolates. Additionally, levels of flavonol glycosides and sinapinic acid esters increased while levels of flavonol diglycosides with glucose attached to the 3-position were reduced. The exogenously administered sinalbin resulted in inhibition of root and hypocotyl growth and markedly influenced metabolite profiles, compared to control and sulfur-deficient plants. These results indicate that, under sulfur deficient conditions, glucosinolates can be a sulfur source for plants. This investigation defines an opportunity to elucidate the mechanism of glucosinolate degradation in vivo. (C) 2011 Elsevier Ltd. All rights reserved.
• Kinetics and substrate specificities of desulfo-glucosinolate sulfotransferases in<i>Arabidopsis thaliana</i>
  作者：Marion Klein、Jutta Papenbrock

  DOI：10.1111/j.1399-3054.2008.01182.x

  日期：2009.2

  Sulfotransferases (SOTs) (EC 2.8.2.‐) catalyze the transfer of a sulfate group from the cosubstrate 3′‐phosphoadenosine 5′‐phosphosulfate (PAPS) to a hydroxyl group of different substrates. In Arabidopsis thaliana, three SOTs were identified to catalyze the last step of glucosinolate (Gl) core structure biosynthesis called AtSOT16, 17 and 18. These enzymes from Arabidopsis ecotype C24 were overexpressed in Escherichia coli and purified by affinity chromatography. Recombinant proteins were used to determine substrate specificities to investigate whether each of the three desulfo (ds)‐Gl SOTs might influence the Gl pattern of Arabidopsis differently. After optimization of the enzyme assay, it was possible to measure in vivo substrates with non‐radioactive PAPS by HPLC analysis of the product. In vitro enzyme assays revealed a preference of AtSOT16 for the indolic ds‐Gl indol‐3‐yl‐methyl, AtSOT17 showed an increased specific activity with increasing chain length of ds‐Gl derived from methionine and AtSOT18 preferred the long‐chain ds‐Gl, 7‐methylthioheptyl and 8‐methylthiooctyl, derived from methionine. In planta ds‐Gl exist side by side; therefore, initial results from one substrate measurements were verified using a defined mixture of ds‐Gl and ds‐Gl/Gl leaf extracts from Arabidopsis ecotype C24. These studies confirmed the one substrate measurements. To compare SOTs from different Arabidopsis ecotypes, additionally, AtSOT18* from ecotype Col‐0 was overexpressed in E. coli and purified. The recombinant protein was used for in vitro measurements and revealed a different enzymatical behavior compared with AtSOT18 from C24. In conclusion, there are differences in the substrate specificities between the three ds‐Gl AtSOT proteins within ecotype C24 and differences among ds‐Gl AtSOT18 proteins from different ecotypes.
• The three desulfoglucosinolate sulfotransferase proteins in Arabidopsis have different substrate specificities and are differentially expressed
  作者：Marion Klein、Michael Reichelt、Jonathan Gershenzon、Jutta Papenbrock

  DOI：10.1111/j.1742-4658.2005.05048.x

  日期：2006.1

  Sulfotransferases (SOTs) catalyse the transfer of a sulfate group from 3′‐phosphoadenosine 5′‐phosphosulfate (PAPS) to an appropriate hydroxy group of various substrates with the parallel formation of 3′‐phosphoadenosine 5′‐phosphate. In Arabidopsis thaliana, 18 SOT proteins (AtSOT) have been identified. Three of them, AtSOT16, AtSOT17 and AtSOT18, catalyse the sulfation of desulfoglucosinolates. The proteins were expressed in Escherichia coli, purified by affinity chromatography and used for enzyme kinetic studies. By establishing two types of enzyme assay using both 35S‐labelled and unlabelled PAPS, separation of the products by HPLC, and detection of the products by monitoring radioactivity or UV absorption, the substrate specificities of the three AtSOT proteins were determined. They show different maximum velocities with several desulfoglucosinolates as substrates and differ in their affinity for desulfobenzylglucosinolate and PAPS. The sequences encoding AtSOT18 were amplified from Arabidopsis ecotypes C24 and Col0; the two expressed proteins differ in two out of 350 amino acids. These amino‐acid variations led to different substrate specificities. Exchange of one of the two amino acids in AtSOT18 from C24 to the respective amino acid in AtSOT18 from Col0 gave the C24 protein the same substrate specificity as the wild‐type AtSOT18 protein from Col0. All three desulfoglucosinolate AtSOT proteins are localized in the cytoplasm, as demonstrated by transient expression of fusion constructs with the green fluorescent protein in Arabidopsis protoplasts. Northern blot analysis indicated differential expression of the three AtSOT genes in plant organs and tissues at different developmental stages and during a light/darkness cycle. High (500 µm) and low (50 µm) sulfate concentrations in the medium did not influence the levels of expression.