[1-15N]-腺嘌呤 | 79364-53-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 咪唑并嘧啶类
• 中文名称: [1-15N]-腺嘌呤
• 英文名称: <1-15N>adenine
• 英文别名: [1-15N]-adenine；[1-15N]adenine；7H-purin-6-amine
• CAS: 79364-53-7
• 化学式: C₅H₅N₅
• 分子量: 136.121
• InChiKey: GFFGJBXGBJISGV-VJJZLTLGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.1
• 重原子数：
  10
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  80.5
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  [1-14C]-D-ribose 、 [1-15N]-腺嘌呤 在 adenylate kinase 、 pyruvate kinase adenine phosphoribosyltransferase 、 5’-三磷酸腺苷 、 magnesium chloride 作用下， 以 phosphate buffer 为溶剂， 反应 16.0h， 生成 ((2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl-1-15N)-3,4-dihydroxytetrahydrofuran-2-yl-5-14C)methyl tetrahydrogen triphosphate
  参考文献：
  名称：

  E. 的过渡状态结构。大肠杆菌tRNA特异性腺苷脱氨酶

  摘要：

  细菌 tRNA 特异性腺苷脱氨酶 (TadA) 在 tRNA 的摆动位置催化腺苷基本脱氨为肌苷，并且是允许单个 tRNA 物种识别多个密码子所必需的。大肠杆菌 TadA 的过渡态结构通过动力学同位素效应 (KIE) 和量子化学计算进行表征。大肠杆菌 tRNA(Arg2) 的茎环用作最小化的 TadA 底物，其腺苷酸编辑位点同位素标记为 [1'-(3)H]、[5'-(3)H2]、[1 '-(14)C], [6-(13)C], [6-(15)N], [6-(13)C, 6-(15)N] 和 [1-(15)N] . [6-(13)C]-, [6-(15)N]-, [1-(15)N]-, [1'- 的本征 KIE 分别为 1.014、1.022、0.994、1.014 和 0.963 (3)H]-、[5'-(3)H2]-分别标记的底物。KIE 套件与具有完整的亲 S 面羟基攻击和几乎完整的 N1 质子化的晚期

  DOI：

  10.1021/ja078008x
• 作为产物：
  描述：

  4-(15N)azanyl-1H-pyrazole-5-carbonitrile 生成 [1-15N]-腺嘌呤
  参考文献：
  名称：

  OHYA, TAKESHI;KANNO, SABURO, CHEMOSPHERE, 19,(1989) N2, C. 1835-1842

  摘要：

  DOI：

文献信息

• Mass spectrometry of nucleic acid constituents. Electron ionization spectra of selectively labeled adenines
  作者：Satinder Sethi、S. P. Gupta、E. E. Jenkins、C. W. Whitehead、Leroy B. Townsend、James A. McCloskey

  DOI：10.1021/ja00376a017

  日期：1982.6
• Transition-State Variation in Human, Bovine, and <i>Plasmodium falciparum</i> Adenosine Deaminases
  作者：Minkui Luo、Vipender Singh、Erika A. Taylor、Vern L. Schramm

  DOI：10.1021/ja072122y

  日期：2007.6.1

  Adenosine deaminases (ADAs) from human, bovine, and Plasmodium falciparum sources were analyzed by kinetic isotope effects (KIEs) and shown to have distinct but related transition states. Human adenosine deaminase (HsADA) is present in most mammalian cells and is involved in B- and T-cell development. The ADA from Plasmodium falciparum (PfADA) is essential in this purine auxotroph, and its inhibition is expected to have therapeutic effects for malaria. Therefore, ADA is of continuing interest for inhibitor design. Stable structural mimics of ADA transition states are powerful inhibitors. Here we report the transition-state structures of PfADA, HsADA, and bovine ADA (BtADA) solved using competitive kinetic isotope effects (KIE) and density functional calculations. Adenines labeled at [6-C-13], [6-N-15], [6-C-13, 6-N-15], and [1-N-15] were synthesized and enzymatically coupled with [1'-C-14] ribose to give isotopically labeled adenosines as ADA substrates for KIE analysis. [6-C-13], [6-N-15], and [1-N-15]adenosines reported intrinsic KIE values of (1.010, 1.011, 1.009), (1.005, 1.005, 1.002), and (1.004, 1.001, 0.995) for PfADA, HsADA, and BtADA, respectively. The differences in intrinsic KIEs reflect structural alterations in the transition states. The [1-N-15] KIEs and computational modeling results indicate that PfADA, HsADA, and BtADA adopt early SNAr transition states, where N1 protonation is partial and the bond order to the attacking hydroxyl nucleophile is nearly complete. The key structural variation among PfADA, HsADA, and BtADA transition states lies in the degree of N1 protonation with the decreased bond lengths of 1.92, 1.55, and 1.28 angstrom, respectively. Thus, PfADA has the earliest and BtADA has the most developed transition state. This conclusion is consistent with the 20-36-fold increase of k(cat) in comparing PfADA with HsADA and BtADA.
• OHYA, TAKESHI;KANNO, SABURO, CHEMOSPHERE, 19,(1989) N2, C. 1835-1842
  作者：OHYA, TAKESHI、KANNO, SABURO

  DOI：——

  日期：——
• Transition State Structure of <i>E. coli t</i>RNA-Specific Adenosine Deaminase
  作者：Minkui Luo、Vern L. Schramm

  DOI：10.1021/ja078008x

  日期：2008.2.1

  rotation occur on the path to the transition state. The late SNAr transition-state established here for E. coli TadA is similar to the late transition state reported for cytidine deaminase. It differs from the early SNAr transition states described recently for the adenosine deaminases from human, bovine, and Plasmodium falciparum sources. The ecTadA transition state structure reveals the detailed architecture

  细菌 tRNA 特异性腺苷脱氨酶 (TadA) 在 tRNA 的摆动位置催化腺苷基本脱氨为肌苷，并且是允许单个 tRNA 物种识别多个密码子所必需的。大肠杆菌 TadA 的过渡态结构通过动力学同位素效应 (KIE) 和量子化学计算进行表征。大肠杆菌 tRNA(Arg2) 的茎环用作最小化的 TadA 底物，其腺苷酸编辑位点同位素标记为 [1'-(3)H]、[5'-(3)H2]、[1 '-(14)C], [6-(13)C], [6-(15)N], [6-(13)C, 6-(15)N] 和 [1-(15)N] . [6-(13)C]-, [6-(15)N]-, [1-(15)N]-, [1'- 的本征 KIE 分别为 1.014、1.022、0.994、1.014 和 0.963 (3)H]-、[5'-(3)H2]-分别标记的底物。KIE 套件与具有完整的亲 S 面羟基攻击和几乎完整的 N1 质子化的晚期