1H-嘌呤-6-胺-8-14C | 5019-49-8

• 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: 1H-嘌呤-6-胺-8-14C
• 英文名称: [8-¹⁴C]adenine
• 英文别名: [14C]-Adenine；1H-Purin-6-amine-8-14C；7H-purin-6-amine
• CAS: 5019-49-8
• 化学式: C₅H₅N₅
• 分子量: 137.117
• InChiKey: GFFGJBXGBJISGV-NJFSPNSNSA-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：

  1H-嘌呤-6-胺-8-14C 、 [(4S,5R)-4-hydroxy-5-(hydroxymethyl)oxolan-2-yl]phosphonic acid 生成 2-脱氧腺苷酸-8-14c
  参考文献：
  名称：

  FILIP, J.;NEJEDLY, Z.;CIHAK, A.;VESELY, J.

  摘要：

  DOI：

文献信息

• The Transition-State Structure for Human MAT2A from Isotope Effects
  作者：Ross S. Firestone、Vern L. Schramm

  DOI：10.1021/jacs.7b05803

  日期：2017.10.4

  inhibitors. We used kinetic isotope effect (KIE), commitment factor (Cf), and binding isotope effect (BIE) measurements combined with quantum mechanical (QM) calculations to solve the transition state structure of human MAT2A. The reaction is characterized by an advanced SN2 transition state. The bond forming from the nucleophilic methionine sulfur to the 5′-C of ATP is 2.03 Å at the transition state (bond

  人甲硫氨酸S-腺苷基转移酶（MAT2A）催化由ATP和甲硫氨酸形成S-腺苷甲硫氨酸（SAM）。合成致死遗传分析已将MAT2A作为缺乏5'-甲基硫代腺苷磷酸化酶（MTAP）表达的肿瘤细胞的抗癌靶标。大约15％的人类癌症是MTAP – / –。其余的可以呈现MTAP -通过MTAP抑制剂。我们将动力学同位素效应（KIE），承诺因子（C f）和结合同位素效应（BIE）测量与量子力学（QM）计算结合使用，以解决人类MAT2A的过渡态结构。该反应的特征在于先进的S N2过渡状态。从亲核蛋氨酸硫到ATP的5'-C形成的键在过渡态（键序为0.67）为2.03Å。ATP的离去基团三磷酸的离解进展顺利，并在ATP的5'-C与三磷酸的氧之间形成2.32Å键（键序为0.23）。MAT2A及其MAT2B调节亚基的相互作用不会导致内在KIE发生变化，表明相同的过渡态结构。与来自大肠杆菌的蛋氨酸腺苷基转移酶的近对称过
• FILIP, J.;NEJEDLY, Z.;CIHAK, A.;VESELY, J.
  作者：FILIP, J.、NEJEDLY, Z.、CIHAK, A.、VESELY, J.

  DOI：——

  日期：——
• NEJEDLY, Z.;FILIP, J.;PEC, V.;KOLINA, J.
  作者：NEJEDLY, Z.、FILIP, J.、PEC, V.、KOLINA, J.

  DOI：——

  日期：——
• Adenine Phosphoribosyltransferase from <i>Sulfolobus solfataricus</i> Is an Enzyme with Unusual Kinetic Properties and a Crystal Structure that Suggests It Evolved from a 6-Oxopurine Phosphoribosyltransferase
  作者：Kaj Frank Jensen、Michael Riis Hansen、Kristine Steen Jensen、Stig Christoffersen、Jens-Christian Navarro Poulsen、Anne Mølgaard、Anders Kadziola

  DOI：10.1021/bi501334m

  日期：2015.4.14

  The adenine phosphoribosyltransferase (APRTase) encoded by the open reading frame SSO2342 of Sulfolobus solfataricus P2 was subjected to crystallographic, kinetic, and ligand binding analyses. The enzyme forms dimers in solution and in the crystals, and binds one molecule of the reactants 5-phosphoribosyl-alpha-1-pyrophosphate (PRPP) and adenine or the product adenosine monophosphate (AMP) or the inhibitor adenosine diphosphate (ADP) in each active site. The individual subunit adopts an overall structure that resembles a 6-oxopurine phosphoribosyltransferase (PRTase) more than known APRTases implying that APRT functionality in Crenarchaeotae has its evolutionary origin in this family of PRTases. Only the N-terminal two-thirds of the polypeptide chain folds as a traditional type I PRTase with a five-stranded beta-sheet surrounded by helices. The C-terminal third adopts an unusual three-helix bundle structure that together with the nucleobase-binding loop undergoes a conformational change upon binding of adenine and phosphate resulting in a slight contraction of the active site. The inhibitor ADP binds like the product AMP with both the alpha- and beta-phosphates occupying the 5'-phosphoribosyl binding site. The enzyme shows activity over a wide pH range, and the kinetic and ligand binding properties depend on both pH and the presence/absence of phosphate in the buffers. A slow hydrolysis of PRPP to ribose 5-phosphate and pyrophosphate, catalyzed by the enzyme, may be facilitated by elements in the C-terminal three-helix bundle part of the protein.