monoheptyl sulfate

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机硫酸及其衍生物
• 英文名称: monoheptyl sulfate
• 英文别名: heptyl sulfate
• 化学式: C₇H₁₅O₄S
• 分子量: 195.26
• InChiKey: MIHVYISIUZTFER-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  2
• 重原子数：
  12
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  74.8
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  monoheptyl sulfate 、 Trospium Chloride 以 氯仿 、 水 为溶剂， 反应 24.0h， 生成
  参考文献：
  名称：

  Langguth; Mutschler, Arzneimittel-Forschung/Drug Research, 1987, vol. 37, # 12, p. 1362 - 1366

  摘要：

  DOI：

文献信息

• Mycobacterium tuberculosis Rv3406 Is a Type II Alkyl Sulfatase Capable of Sulfate Scavenging
  作者：Kimberly M. Sogi、Zev J. Gartner、Mark A. Breidenbach、Mason J. Appel、Michael W. Schelle、Carolyn R. Bertozzi

  DOI：10.1371/journal.pone.0065080

  日期：——

  α-ketoglutarate-dependent dioxygenase that catalyzes the oxidation and subsequent cleavage of alkyl sulfate esters. Rv3406 was identified based on its homology to the alkyl sulfatase AtsK from Pseudomonas putida. Using an in vitro biochemical assay, we confirmed that Rv3406 is a sulfatase with a preference for alkyl sulfate substrates similar to those processed by AtsK. We determined the crystal structure

  结核分枝杆菌 (Mtb) 的基因组编码 9 种假定的硫酸酯酶，其中没有一种具有已知的功能或底物。在这里，我们将 Mtb 的单一推定 II 型硫酸酯酶 Rv3406 表征为非血红素铁 (II) 和 α-酮戊二酸依赖性双加氧酶，可催化烷基硫酸酯的氧化和随后的裂解。Rv3406 是根据其与恶臭假单胞菌的烷基硫酸酯酶 AtsK 的同源性进行鉴定的。使用体外生化分析，我们证实 Rv3406 是一种硫酸酯酶，偏好与 AtsK 处理的那些类似的烷基硫酸盐底物。我们确定了 2.5 Å 的 apo Rv3406 硫酸酯酶的晶体结构。Rv3406 和 AtsK 的活性位点残基基本上是可叠加的，表明这两种硫酸酯酶具有相同的催化机制。最后，我们在 Mtb 中产生了一个 Rv3406 突变体（Δrv3406）来研究硫酸酯酶在清除硫酸盐中的作用。与野生型 Mtb 或补充菌株相比，Δrv3406 菌株在以 2-乙基己基
• Characterization of a Sulfur-regulated Oxygenative Alkylsulfatase from Pseudomonas putida S-313
  作者：Antje Kahnert、Michael A. Kertesz

  DOI：10.1074/jbc.m005820200

  日期：2000.10

  The atsK gene of Pseudomonas putida S-313 was required for growth with alkyl sulfate esters as sulfur source. The AtsK protein was overexpressed in Escherichia coli and purified to homogeneity. Sequence analysis revealed that AtsK was closely related to E. coli taurine dioxygenase (38% amino acid identity). The AtsK protein catalyzed the alpha-ketoglutarate-dependent cleavage of a range of alkyl sulfate esters, with chain lengths ranging from C-4 to C-12, required oxygen and Fe2+ for activity and released succinate, sulfate, and the corresponding aldehyde as products. Enzyme activity was optimal at pH 7 and was strongly stimulated by ascorbate. Unlike most other characterized alpha-ketoglutarate-dependent dioxygenases, AtsK accepted a range of alpha-keto acids as co-substrates, including alpha-ketoglutarate (K-m 140 mu M), alpha-ketoadipate, alpha-ketovalerate, and alpha-ketooctanoate. The measured K-m values for hexyl sulfate and SDS were 40 and 34 mu M, respectively. The apparent M-r of the purified enzyme of 121,000 was consistent with a homotetrameric structure, which is unusual for this enzyme superfamily, members of which are usually monomeric or dimeric, The properties and amino acid sequence of the AtsK enzyme thus define it as an unusual oxygenolytic alkylsulfatase and a novel member of the alpha-ketoglutarate-dependent dioxygenase family.
• Langguth; Mutschler, Arzneimittel-Forschung/Drug Research, 1987, vol. 37, # 12, p. 1362 - 1366
  作者：Langguth、Mutschler

  DOI：——

  日期：——