Tungstate | 51682-10-1

• 分子结构分类: 无机化合物 - 混合金属/非金属化合物 - 各种混合金属/非金属
• 英文名称: Tungstate
• 英文别名: dioxido(dioxo)tungsten
• CAS: 51682-10-1；12737-86-9
• 化学式: O4W-2
• 分子量: 247.84
• InChiKey: PBYZMCDFOULPGH-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.62
• 重原子数：
  5
• 可旋转键数：
  0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  80.3
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  Molybdopterin adenine dinucleotide(3-) 、 氢(+1)阳离子 、 Tungstate 生成 adenosine 5'-monophosphate 、 水 、 W-molybdopterin cofactor
  参考文献：
  名称：

  Function of MoaB Proteins in the Biosynthesis of the Molybdenum and Tungsten Cofactors

  摘要：

  Molybdenum (Mo) and tungsten (W) enzymes catalyze important redox reactions in the global carbon, nitrogen, and sulfur cycles. Except in nitrogenases both metals are exclusively associated with a unique metal-binding pterin (MPT) that is synthesized by a conserved multistep biosynthetic pathway, which ends with the insertion and thereby biological activation of the respective element.' Although the biosynthesis of Mo cofactors has been intensively studied in various systems, the biogenesis of W-containing enzymes, mostly found in archaea, is poorly understood. Here, we describe the function of the Pyrococcus furiosus MoaB protein that is homologous to bacteria (such as MogA) and eukaryotic proteins (such as Cnx1) involved in the final steps of Mo cofactor synthesis. MoaB reconstituted the function of the homologous Escherichia coli MogA protein and catalyzes the adenylylation of MPT in a Mg2+ and ATP-dependent way. At room temperature reaction velocity was similar to that of the previously described plant Cnx1G domain, but it was increased up to 20-fold at 80 degrees C. Metal and nucleotide specificity for MPT adenylylation is well conserved between W and Mo cofactor synthesis. Thermostability of MoaB is believed to rely on its hexameric structure, whereas homologous mesophilic MogA-related proteins form trimers. Comparison of P. furiosus MoaB to E. coli MoaB and MogA revealed that only MogA is able to catalyze MPT adenylylation, whereas E. coli MoaB is inactive. In summary, MogA, Cnx1G, and MoaB proteins exhibit the same adenylyl transfer activity essential for metal insertion in W or Mo cofactor maturation.

  DOI：

  10.1021/bi7020487
• 作为试剂：
  描述：

  、 D-tartrate 、 、 2,3-二羟基-[R-(R*,R*)]-丁二酸二钠盐 、 Calcium d-tartrate 、 硫酸 在 Tungstate 作用下， 生成 D-酒石酸
  参考文献：
  名称：

  Process for preparing CIS-epoxysuccinic acid salts of high purity

  摘要：

  高纯度顺式环氧琥珀酸及其盐通过在特定条件下，将在钨酸盐或钼酸盐催化剂存在下反应马来酸盐和过氧化氢得到的水溶液与强碱性II型阴离子交换树脂接触，经济而系统地制备。

  公开号：

  US04065475A1

文献信息

• Function of MoaB Proteins in the Biosynthesis of the Molybdenum and Tungsten Cofactors
  作者：Loes E. Bevers、Peter-Leon Hagedoorn、José A. Santamaria-Araujo、Axel Magalon、Wilfred R. Hagen、Guenter Schwarz

  DOI：10.1021/bi7020487

  日期：2008.1.1

  Molybdenum (Mo) and tungsten (W) enzymes catalyze important redox reactions in the global carbon, nitrogen, and sulfur cycles. Except in nitrogenases both metals are exclusively associated with a unique metal-binding pterin (MPT) that is synthesized by a conserved multistep biosynthetic pathway, which ends with the insertion and thereby biological activation of the respective element.' Although the biosynthesis of Mo cofactors has been intensively studied in various systems, the biogenesis of W-containing enzymes, mostly found in archaea, is poorly understood. Here, we describe the function of the Pyrococcus furiosus MoaB protein that is homologous to bacteria (such as MogA) and eukaryotic proteins (such as Cnx1) involved in the final steps of Mo cofactor synthesis. MoaB reconstituted the function of the homologous Escherichia coli MogA protein and catalyzes the adenylylation of MPT in a Mg2+ and ATP-dependent way. At room temperature reaction velocity was similar to that of the previously described plant Cnx1G domain, but it was increased up to 20-fold at 80 degrees C. Metal and nucleotide specificity for MPT adenylylation is well conserved between W and Mo cofactor synthesis. Thermostability of MoaB is believed to rely on its hexameric structure, whereas homologous mesophilic MogA-related proteins form trimers. Comparison of P. furiosus MoaB to E. coli MoaB and MogA revealed that only MogA is able to catalyze MPT adenylylation, whereas E. coli MoaB is inactive. In summary, MogA, Cnx1G, and MoaB proteins exhibit the same adenylyl transfer activity essential for metal insertion in W or Mo cofactor maturation.