imidazoleglycerol phosphate | 36244-87-8

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机磷酸及其衍生物
• 英文名称: imidazoleglycerol phosphate
• 英文别名: phosphoric acid mono-[(2R,3S)-2,3-dihydroxy-3-(1(3)H-imidazol-4-yl)-propyl ester]；Phosphorsaeure-mono-[(2R,3S)-2,3-dihydroxy-3-(1(3)H-imidazol-4-yl)-propylester]；[(2R,3S)-2,3-dihydroxy-3-(1H-imidazol-5-yl)propyl] dihydrogen phosphate
• CAS: 36244-87-8
• 化学式: C₆H₁₁N₂O₆P
• 分子量: 238.137
• InChiKey: HFYBTHCYPKEDQQ-RITPCOANSA-N

物化性质

• 沸点：
  708.6±70.0 °C(Predicted)
• 密度：
  1.804±0.06 g/cm3(Predicted)
• 物理描述：
  Solid

计算性质

• 辛醇/水分配系数(LogP)：
  -3.2
• 重原子数：
  15
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  136
• 氢给体数：
  5
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  imidazoleglycerol phosphate 在 三乙醇胺 、 重水 作用下， 反应 23.0h， 生成 <2,3,3-2H3>-histidinol
  参考文献：
  名称：

  Escherichia coli imidazoleglycerol phosphate dehydratase: spectroscopic characterization of the enzymic product and the steric course of the reaction

  摘要：

  Recombinant strains of Escherichia coli have been developed for the high-level production of imidazoleglycerol phosphate dehydratase (IGPD) and imidazoleacetol phosphate aminotransferase (IAP aminotransferase). These protein sources facilitated the determination of the IGPD reaction stereochemistry and enabled the development of a continuous spectrophotometric enzyme assay for the IGPD reaction. D-erythro-IGP and D-erythro-[3-H-2]IGP were generated using a chemoenzymatic approach. D-((-))-[3-H-2]Ribose5-phosphate was prepared synthetically, starting from diacetone-D-glucose, and converted enzymatically to D-erythro-[3-H-2]IGP. In separate reactions, D-erythro-IGP and D-erythro-[3-H-2]IGP were converted to IAP using E. coli IGPD, The resulting IAP was transformed directly to histidinol using the coupled activities of E, coli IAP aminotransferase and histidinol phosphate phosphatase. The enzymatically generated histidinol samples were analyzed by H-1 and 2H NMR and compared to a synthetically prepared sample of (2S*,3S*)-[3-H-2]histidinol. This analysis demonstrated that the E. coli IGPD reaction proceeds with inversion of configuration at C-3, and the proton added to C-3 of IAP during the course of the dehydration is derived from the solvent. The observed stereochemical outcome is consistent with the idea that if the IGPD reaction proceeds through an enol intermediate, then tautomerization of the enol to IAP must be enzyme-mediated, The product of the IGPD reaction, IAP, has been characterized by NMR spectroscopy in aqueous solution. IAP undergoes rapid exchange of the C-3 protons with the bulk medium and exists as a mixture of the ketone and its hydrate (a geminal diol). Additional solution chemistry of IAP was observed using UV-vis and EPR spectroscopy and is consistent with the idea that IAP coordinates to Mn2+ in a bi- or tridentate fashion in aqueous solutions.

  DOI：

  10.1021/ja00148a001
• 作为产物：
  描述：

  甲脒盐酸盐 、 alkaline earth salt of/the/ methylsulfuric acid 生成 imidazoleglycerol phosphate
  参考文献：
  名称：

  Ames, Journal of Biological Chemistry, 1957, vol. 228, p. 131,135

  摘要：

  DOI：

文献信息

• Escherichia coli imidazoleglycerol phosphate dehydratase: spectroscopic characterization of the enzymic product and the steric course of the reaction
  作者：Aulma R. Parker、Jeffrey A. Moore、John M. Schwab、V. Jo Davisson

  DOI：10.1021/ja00148a001

  日期：1995.11

  Recombinant strains of Escherichia coli have been developed for the high-level production of imidazoleglycerol phosphate dehydratase (IGPD) and imidazoleacetol phosphate aminotransferase (IAP aminotransferase). These protein sources facilitated the determination of the IGPD reaction stereochemistry and enabled the development of a continuous spectrophotometric enzyme assay for the IGPD reaction. D-erythro-IGP and D-erythro-[3-H-2]IGP were generated using a chemoenzymatic approach. D-((-))-[3-H-2]Ribose5-phosphate was prepared synthetically, starting from diacetone-D-glucose, and converted enzymatically to D-erythro-[3-H-2]IGP. In separate reactions, D-erythro-IGP and D-erythro-[3-H-2]IGP were converted to IAP using E. coli IGPD, The resulting IAP was transformed directly to histidinol using the coupled activities of E, coli IAP aminotransferase and histidinol phosphate phosphatase. The enzymatically generated histidinol samples were analyzed by H-1 and 2H NMR and compared to a synthetically prepared sample of (2S*,3S*)-[3-H-2]histidinol. This analysis demonstrated that the E. coli IGPD reaction proceeds with inversion of configuration at C-3, and the proton added to C-3 of IAP during the course of the dehydration is derived from the solvent. The observed stereochemical outcome is consistent with the idea that if the IGPD reaction proceeds through an enol intermediate, then tautomerization of the enol to IAP must be enzyme-mediated, The product of the IGPD reaction, IAP, has been characterized by NMR spectroscopy in aqueous solution. IAP undergoes rapid exchange of the C-3 protons with the bulk medium and exists as a mixture of the ketone and its hydrate (a geminal diol). Additional solution chemistry of IAP was observed using UV-vis and EPR spectroscopy and is consistent with the idea that IAP coordinates to Mn2+ in a bi- or tridentate fashion in aqueous solutions.
• Ames, Journal of Biological Chemistry, 1957, vol. 228, p. 131,135
  作者：Ames

  DOI：——

  日期：——