glucobrassicin | 47628-38-6

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: glucobrassicin
• 英文别名: Glucobrassicin(1-)；[[2-(1H-indol-3-yl)-1-[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]sulfanylethylidene]amino] sulfate
• CAS: 47628-38-6
• 化学式: C₁₆H₁₉N₂O₉S₂
• 分子量: 447.467
• InChiKey: DNDNWOWHUWNBCK-JZYAIQKZSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -0.2
• 重原子数：
  29
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  218
• 氢给体数：
  5
• 氢受体数：
  11

反应信息

• 作为产物：
  描述：

  PAPS 、 desulfoglucobrassicin 生成 Adenosine 3',5'-bismonophosphate(4-) 、 glucobrassicin 、 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

文献信息

• A radioassay of enzymes catalyzing the glucosylation and sulfation steps of glucosinolate biosynthesis in Brassica species
  作者：J.C. Jain、D.W. Reed、J.W.D. GrootWassink、E.W. Underhill

  DOI：10.1016/0003-2697(89)90369-2

  日期：1989.4

  A new method for assaying the enzymes uridine diphosphoglucose (UDPglucose):thiohydroximate glucosyltransferase and 3'-phosphoadenosine-5'-phosphosulfate:desulfoglucosinolate sulfotransferase has been designed. The assay system is based on the separation of nonionic [14C]desulfobenzylglucosinolate from anionic [14C]UDPglucose and anionic [14C]benzylglucosinolate, respectively, by differential adsorption

  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。
• 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.
• 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.