Mg(adenosine triphosphate) ^2-

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷酸
• 英文名称: Mg(adenosine triphosphate) ^2-
• 英文别名: MgATP ^2-；Mg(2+)-ATP；MgATP(2-)；magnesium;[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-oxidophosphoryl]oxy-oxidophosphoryl] phosphate
• 化学式: C₁₀H₁₂N₅O₁₃P₃*Mg
• 分子量: 527.457
• InChiKey: CYYJCOXYBYJLIK-MCDZGGTQSA-J

计算性质

• 辛醇/水分配系数(LogP)：
  -4.54
• 重原子数：
  32
• 可旋转键数：
  7
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  290
• 氢给体数：
  3
• 氢受体数：
  17

反应信息

• 作为产物：
  描述：

  adenosine 5'-triphosphate 在 magnesium chloride 作用下， 以 水 为溶剂， 生成 Mg(adenosine triphosphate) ^2-
  参考文献：
  名称：

  323.15 至 398.15 K 腺苷 5-二磷酸和腺苷 5-三磷酸与 Mg2+ 相互作用的热力学参数

  摘要：

  已在 323.15、348.15、373.15 和 398.15 K（ATP）和 348.15 和 373.15 K（ADP）与 Mg2+ 水中的 5'-二磷酸腺苷（ADP）和 5'-三磷酸腺苷（ATP）相互作用 Mg2+ 与ADP 和ATP 的反应焓是由ADP 和ATP 的四甲基铵盐水溶液与MgCl2 溶液在等温流动热量计中混合的热量获得的。计算了相互作用的平衡常数 (K)、焓变 (ΔH°)、熵变 (ΔS°) 和热容变化 (ΔCp°) 值：Mg2++Ln−=MgL2−n 和 Mg2++MgL2− n=Mg2L4−n，其中对于 L=ATP，n=4，对于 L=ADP，n=3。结果与较低温度下的结果一致。对于研究的两种核苷酸，上述两种反应在研究的温度范围内是吸热和熵驱动的。Mg2+ 与 ADP 与 ATP 相互作用的大 ΔCp° 值表明核苷酸的磷酸基团参与了 Mg2+ 的配位。第一个和第二个 Mg2+

  DOI：

  10.1007/bf00973517

文献信息

• Thermodynamic parameters for the interaction of adenosine 5?-diphosphate, and adenosine 5?-triphosphate with Mg2+ from 323.15 to 398.15 K
  作者：P. Wang、J. L. Oscarson、R. M. Izatt、G. D. Watt、C. D. Larsen

  DOI：10.1007/bf00973517

  日期：1995.10

  The interaction of adenosine 5′-diphosphate (ADP) and adenosine 5′-triphosphate (ATP) with Mg2+ in water has been studied calorimetrically at 323.15, 348.15, 373.15, and 398.15 K for ATP and at 348.15 and 373.15 K for ADP. The enthalpies of reaction of Mg2+ with ADP and ATP were obtained from the heats of mixing of aqueous solutions of tetramethylammonium salts of ADP and ATP with MgCl2 solutions in

  已在 323.15、348.15、373.15 和 398.15 K（ATP）和 348.15 和 373.15 K（ADP）与 Mg2+ 水中的 5'-二磷酸腺苷（ADP）和 5'-三磷酸腺苷（ATP）相互作用 Mg2+ 与ADP 和ATP 的反应焓是由ADP 和ATP 的四甲基铵盐水溶液与MgCl2 溶液在等温流动热量计中混合的热量获得的。计算了相互作用的平衡常数 (K)、焓变 (ΔH°)、熵变 (ΔS°) 和热容变化 (ΔCp°) 值：Mg2++Ln−=MgL2−n 和 Mg2++MgL2− n=Mg2L4−n，其中对于 L=ATP，n=4，对于 L=ADP，n=3。结果与较低温度下的结果一致。对于研究的两种核苷酸，上述两种反应在研究的温度范围内是吸热和熵驱动的。Mg2+ 与 ADP 与 ATP 相互作用的大 ΔCp° 值表明核苷酸的磷酸基团参与了 Mg2+ 的配位。第一个和第二个 Mg2+
• Tajmir-Riahi, H. A.; Bertrand, M. J.; Theophanides, T., Canadian Journal of Chemistry, 1986, vol. 64, p. 960 - 966
  作者：Tajmir-Riahi, H. A.、Bertrand, M. J.、Theophanides, T.

  DOI：——

  日期：——
• Energetic Effects of Magnesium in the Recognition of Adenosine Nucleotides by the F₁-ATPase β Subunit
  作者：Nancy O. Pulido、Guillermo Salcedo、Gerardo Pérez-Hernández、Concepción José-Núñez、Adrián Velázquez-Campoy、Enrique García-Hernández

  DOI：10.1021/bi1006767

  日期：2010.6.29

  Nucleotide-induced conformational changes of the catalytic beta subunits play a crucial role in the rotary mechanism of F-1-ATPase. To gain insights into the energetic bases that govern the recognition of nucleotides by the isolated beta subunit from thermophilic Bacillus PS3 (T beta), the binding of this monomer to Mg(II)-free and Mg(II)-bound adenosine nucleotides was characterized using high-precision isothermal titration calorimetry. The interactions of Mg(II) with free ATP or ADP were also measured calorimetrically. A model that considers simultaneously the interactions of T beta with Mg.ATP or with ATP and in which ATP is able to bind two Mg(II) atoms sequentially was used to determine the formation parameters of the T beta-Mg.ATP complex from calorimetric data, This analysis yielded significantly different Delta H-b and Delta S-b values in relation to those obtained using a single-binding site model, while Delta G(b) was almost unchanged. Published calorimetric data for the titration of T beta with Mg.ADP [Perez-Hernandez, G., et al. (2002) Arch. Biochem. Biophys. 408.177-183] were reanalyzed with the ternary model to determine the corresponding true binding parameters. Interactions of T beta with Mg.ATP, ATP, Mg.ADP, or ADP were enthalpically driven. Larger differences in thermodynamic properties were observed between T beta-Mg.ATP and T beta-ATP complexes than between T beta-Mg.ADP and T beta-ADP complexes or between T beta-Mg.ATP and T beta-Mg.ADP complexes. These binding data, in conjunction with those for the association of Mg(II) with free nucleotides, allowed for a determination of the energetic effects of the metal ion on the recognition of adenosine nucleotides by T beta [i.e., T beta.AT(D)P + Mg(II) reversible arrow T beta.AT(D)P-Mg]. Because of a more favorable binding enthalpy, Mg(II) is recognized more avidly by the T beta.ATP complex, indicating better stereochemical complementarity than in the T beta.ADP complex. Furthermore, a structural-energetic analysis suggests that T beta adopts a more closed conformation when it is bound to Mg.ATP than to ATP or Mg.ADP, in agreement with recently published NMR data [Yagi. H., et al. (2009) J. Biol. Chem. 284, 2374-2382]. Using published binding data, a similar analysis of Mg(II) energetic effects was performed for the free energy change of F-1 catalytic sites, in the framework of bi- or tri-site binding models.