α-D-mannopyranosyl 2,4-dinitrophenyl phosphate | 138385-94-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: α-D-mannopyranosyl 2,4-dinitrophenyl phosphate
• 英文别名: α-D-mannopyranosyl (tri-n-butylammonium) 2,4-dinitrophenyl phosphate
• CAS: 138385-94-1
• 化学式: C₁₂H₁₅N₂O₁₃P*C₁₂H₂₇N
• 分子量: 611.584
• InChiKey: IRAYTWSGZDDMSW-BTIVEGDLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.49
• 重原子数：
  41.0
• 可旋转键数：
  16.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  235.43
• 氢给体数：
  5.0
• 氢受体数：
  13.0

反应信息

• 作为产物：
  描述：

  2,4-二硝基酚 、 α-D-mannopyranosyl (bis(cyclohexylammonium)phosphate) 在 三正丁胺 、 Dowex 50W-X₈ 、 N,N'-二环己基碳二亚胺 作用下， 生成 α-D-mannopyranosyl 2,4-dinitrophenyl phosphate
  参考文献：
  名称：

  Synthesis and testing of sugar phosphofluoridates and cyclic phosphates as inhibitors of phosphoglucomutase

  摘要：

  Three aldose phosphofluoridates, D-glucose 6-phosphofluoridate, alpha-D-mannopyranosyl phosphofluoridate, and 2-deoxy-2-fluoro-alpha-D-glucopyranosyl phosphofluoridate, have been synthesized from the parent phosphate and 2,4-dinitrofluorobenzene, and the mechanism of fluorination has been investigated. Another modified aldose phosphate, alpha-D-glucopyranosyl 4,6-cyclic phosphate [phosphate] has also been synthesized as an analogue of 6-phospho-alpha-D-glucopyranosyl phosphate. These compounds were tested as possible mechanism-based inactivators of rabbit muscle phosphoglucomutase, but no time-dependent inactivation was observed. They were, however, found to be reversible inhibitors of phosphoglucomutase, and comparison of their dissociation constants with those of the parent phosphates revealed that the removal of a single negative charge weakens ground-state binding by approximately 11 kJ/mol. Further, the absence of any detectable phosphorylation of these analogues reveals that this second charge is even more important for transition-state interaction, contributing at least 40 kJ/mol to transition-state stability. This suggests that the parent substrates bind to the enzyme and react in their dianionic forms, and it provides a measure of the value of charge-charge interactions at the active site of this key metabolic enzyme.

  DOI：

  10.1021/jo00029a007