(3aR,5R,6R,6aR)-5-((R)-hydroxymethyl-d)-2,2-dimethyltetrahydrofuro[2,3-d][1,3]dioxol-6-ol | 1013943-43-5

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (3aR,5R,6R,6aR)-5-((R)-hydroxymethyl-d)-2,2-dimethyltetrahydrofuro[2,3-d][1,3]dioxol-6-ol
• CAS: 1013943-43-5
• 化学式: C₈H₁₄O₅
• 分子量: 191.188
• InChiKey: JAUQZVBVVJJRKM-WZLHGHLMSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.78
• 重原子数：
  13.0
• 可旋转键数：
  1.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  68.15
• 氢给体数：
  2.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  (3aR,5R,6R,6aR)-5-((R)-hydroxymethyl-d)-2,2-dimethyltetrahydrofuro[2,3-d][1,3]dioxol-6-ol 在 Dowex-50W 作用下， 以 水 为溶剂， 生成 (5R)-[5-²H1]ribose
  参考文献：
  名称：

  氨基咪唑核苷酸形成厌氧 5-羟基苯并咪唑：硫胺素和维生素 B12 生物合成的意外交叉点

  摘要：

  细菌硫胺嘧啶合酶 (thiC) 的比较基因组学揭示了 thiC (bzaF) 的旁系同源物与厌氧维生素 B12 生物合成基因聚集在一起。在此，我们证明 BzaF 是一种自由基 S-腺苷甲硫氨酸酶，可催化氨基咪唑核苷酸 (AIR) 显着转化为 5-羟基苯并咪唑 (5-HBI)。我们确定了关键产物原子的起源并提出了反应机制。这些研究代表了解决厌氧维生素 B12 组装中长期存在的问题的第一步，并揭示了硫胺素和维生素 B12 生物合成的意外交叉。

  DOI：

  10.1021/jacs.5b03576
• 作为产物：
  描述：

  3-O-benzyl-1,2-O-isopropylidene-α-D-ribo-pentodialdo-1,4-furanose 在 溴丁基-镁 、 monodeuterioisoborneol 、 偶氮二甲酸二异丙酯 、 palladium on activated charcoal 、 potassium carbonate 、 溶剂黄146 、 三苯基膦 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 生成 (3aR,5R,6R,6aR)-5-((R)-hydroxymethyl-d)-2,2-dimethyltetrahydrofuro[2,3-d][1,3]dioxol-6-ol
  参考文献：
  名称：

  氨基咪唑核苷酸形成厌氧 5-羟基苯并咪唑：硫胺素和维生素 B12 生物合成的意外交叉点

  摘要：

  细菌硫胺嘧啶合酶 (thiC) 的比较基因组学揭示了 thiC (bzaF) 的旁系同源物与厌氧维生素 B12 生物合成基因聚集在一起。在此，我们证明 BzaF 是一种自由基 S-腺苷甲硫氨酸酶，可催化氨基咪唑核苷酸 (AIR) 显着转化为 5-羟基苯并咪唑 (5-HBI)。我们确定了关键产物原子的起源并提出了反应机制。这些研究代表了解决厌氧维生素 B12 组装中长期存在的问题的第一步，并揭示了硫胺素和维生素 B12 生物合成的意外交叉。

  DOI：

  10.1021/jacs.5b03576

文献信息

• Mechanistic Studies on Pyridoxal Phosphate Synthase:  The Reaction Pathway Leading to a Chromophoric Intermediate
  作者：Jeremiah W. Hanes、Kristin E. Burns、David G. Hilmey、Abhishek Chatterjee、Pieter C. Dorrestein、Tadhg P. Begley

  DOI：10.1021/ja076604l

  日期：2008.3.1

  Two routes for the de novo biosynthesis of pyridoxal-5'-phosphate (PLP) have been discovered and reconstituted in vitro. The most common pathway that organisms use is dependent upon the activity of just two enzymes, known as Pdx1 (YaaD) and Pdx2 (YaaE) in bacteria. Pdx2 has been shown to have glutaminase activity and most likely channels ammonia to the active site of the PLP synthase subunit, Pdx1, where ribose-5-phosphate (R5P), glyceraldehyde-3-phosphate (G3P), and ammonia are condensed in a complex series of reactions. In this report we investigated the early steps in the mechanism of PLP formation. Under pre-steady-state conditions, a chromophoric intermediate (I-320) is observed that accumulates upon addition of only two of the substrates, R5P and glutamine. The intermediate is covalently bound to the protein. We synthesized C5 monodeuterio (pro-R, pro-S) and dideuterio R5P and showed that there is a primary kinetic isotope effect on the formation of this intermediate using the pro-R but not the pro-S labeled isomer. Furthermore, it was shown that the phosphate unit of R5P is eliminated rather than hydrolyzed in route to intermediate formation and also that there is an observed C5-deuterium kinetic isotope effect on this elimination step. Interestingly, it was observed that the formation of the intermediate could be triggered in the absence of Pdx2 by the addition of high concentrations of NH4Cl to a preincubated solution of Pdx1 and R5P. The formation of I-320 was also monitored using high-resolution electrospray ionization Fourier transform mass spectrometry and revealed a species of mass 34 304 Da (Pdx1 + 95 Da). These results allow us to narrow the mechanistic possibilities for the complex series of reactions involved in PLP formation.