Pyridinium, 3-carboxy-1-(5-O-phosphono-beta-D-ribofuranosyl)-, inner salt

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 吡啶核苷酸
• 英文名称: Pyridinium, 3-carboxy-1-(5-O-phosphono-beta-D-ribofuranosyl)-, inner salt
• 英文别名: [(2S,3R,4S,5S)-5-(3-carboxypyridin-1-ium-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl hydrogen phosphate
• 化学式: C₁₁H₁₄NO₉P
• 分子量: 335.207
• InChiKey: JOUIQRNQJGXQDC-XKNYDFJKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.8
• 重原子数：
  22
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.45
• 拓扑面积：
  161
• 氢给体数：
  4
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  对甲酚 、 Pyridinium, 3-carboxy-1-(5-O-phosphono-beta-D-ribofuranosyl)-, inner salt 在 Sporomusa ovata nicotinate mononucleotide:phenol/p-cresol phosphoribosyltransferase 、 水 、 聚甘氨酸 作用下， 以 乙醇 为溶剂， 生成 烟酸 、
  参考文献：
  名称：

  Structural Insights into the Function of the Nicotinate Mononucleotide:phenol/p-cresol Phosphoribosyltransferase (ArsAB) Enzyme from Sporomusa ovata

  摘要：

  Cobamides (Cbas) are cobalt (Co) containing tetrapyrrole-derivatives involved in enzyme-catalyzed carbon skeleton rearrangements, methyl-group transfers, and reductive dehalogenation. The biosynthesis of cobamides is complex and is only performed by some bacteria and achaea. Cobamides have an upper (CO beta) ligand (5'-deoxyadenosyl or methyl) and a lower (Co alpha) ligand base that contribute to the axial Co coordinations. The identity of the lower Co alpha ligand varies depending on the organism synthesizing the Cbas. The homoacetogenic bacterium Sporomusa ovata synthesizes two unique phenolic cobamides (i.e., Co alpha-(phenolyl/p-cresolyl)-cobamide), which are used in the catabolism of methanol and 3,4-dimethoxybenzoate by this bacterium. The S. ovata ArsAB enzyme activates a phenolic lower ligand prior to its incorporation into the cobamide. ArsAB consists of two subunits, both of which are homologous (similar to 35% identity) to the well-characterized Salmonella enterica CobT enzyme, which transfers nitrogenous bases such as 5,6-dimethylbenzimidazole (DMB) and adenine, but cannot utilize phenolics. Here we report the threedimensional structure of ArsAB, which shows that the enzyme forms a pseudosymmetric heterodimer, provide evidence that only the ArsA subunit has base:phosphoribosyl-transferase activity, and propose a mechanism by which phenolic transfer is facilitated by an activated water molecule.

  DOI：

  10.1021/bi301142h