5-脱氧-8,5-环腺苷酸 | 3415-89-2

• 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: 5-脱氧-8,5-环腺苷酸
• 英文名称: 8,5'-Anhydroadenosine
• 英文别名: desoxy-5' cyclo-5',8 adenosine；5'-deoxy-5',8-cycloadenosine；5'-deoxy-8,5'-cycloadenosine；5',8-anhydroadenosine；8,5'-anhydroadenosine；5',8-cycloadenosine；(1R,12R,13S,14R)-7-amino-15-oxa-2,4,6,9-tetrazatetracyclo[10.2.1.02,10.03,8]pentadeca-3,5,7,9-tetraene-13,14-diol
• CAS: 3415-89-2
• 化学式: C₁₀H₁₁N₅O₃
• 分子量: 249.229
• InChiKey: HQTVJWSZGWEZPW-KAFVXXCXSA-N

物化性质

• 沸点：
  672.3±55.0 °C(Predicted)
• 密度：
  2.43±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -1.7
• 重原子数：
  18
• 可旋转键数：
  0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  119
• 氢给体数：
  3
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  O-isopropylidene-2',3' N,N'-dibenzoyl-6 dihydro-7,8 cyclo-5',8 desoxy-5 adenosine 在 盐酸 、 soude methanolique 0.5N 作用下， 反应 8.0h， 生成 5-脱氧-8,5-环腺苷酸
  参考文献：
  名称：

  Synthese de la cyclo-5'-8 desoxy-5' adenosine: stereochimie et mecanisme de la cyclisation d'un derive de l'iodo-5' adenosine par le zinc

  摘要：

  DOI：

  10.1016/s0040-4020(01)83125-2

文献信息

• Thermolysis of the CoC bond in adenosylcobalamin (coenzyme B12)—IV. Products, kinetics and CoC bond dissociation energy studies in ethylene glycol
  作者：Benjamin P. Hay、Richard G. Finke

  DOI：10.1016/s0277-5387(00)81775-1

  日期：1988.1

  trap TEMPO proceeds with four isosbestic points to yield 100±2% Co(II)B 12 and two nucleoside products, 8,5′-anhydroadenosine and 5′-deoxyadenosine. In the presence of >10 −2 M TEMPO, the TEMPO-trapped Ado . product (T-Ado) and Co(II)B 12 account quantitatively for the starting AdoB 12 . From HPLC studies of the concentration of the nucleoside products vs [TEMPO], absolute rate constants at 110°C for

  摘要在引言概述了腺苷钴胺素（AdoB 12）键均解问题的关键问题之后，介绍了AdoB 12在乙二醇中热解的产物，动力学和CoC5'键解离能的详细信息。在不存在氮氧自由基捕获器TEMPO的情况下，AdoB 12的厌氧热解进行四个同构异构点，得到100±2％Co（II）B 12和两个核苷产物，8,5'-脱水腺苷和5'-脱氧腺苷。在> 10 -2 M TEMPO的情况下，TEMPO陷获的Ado。产物（T-Ado）和Co（II）B 12在数量上占起始AdoB 12的比例。通过HPLC研究核苷产物的浓度与[TEMPO]的关系，得出Ado在110°C时的绝对速率常数。环化及其H。首次从乙二醇溶剂中提取 kc（110℃）≤5×10 5 s -1和ka（110℃）≤7×10 3 M -1 s -1。在添加真实的Co（II）B 12的情况下进行的动力学研究表明，1 / [Kobs与[Co（II）B 12]
• Gani, David; Hollaway, Michael R.; Johnson, Alan W., Journal of Chemical Research, Miniprint, 1981, # 7, p. 2327 - 2344
  作者：Gani, David、Hollaway, Michael R.、Johnson, Alan W.、Lappert, Michael F.、Wallis, O. Caryl

  DOI：——

  日期：——
• Thermolysis of the cobalt-carbon bond of adenosylcobalamin. 2. Products, kinetics, and cobalt-carbon bond dissociation energy in aqueous solution
  作者：Benjamin P. Hay、Richard G. Finke

  DOI：10.1021/ja00276a020

  日期：1986.8
• Synthesis and Characterization of 3‘,4‘-Anhydroadenosylcobalamin:  A Coenzyme B₁₂ Analogue with Unusual Properties
  作者：Olafur Th. Magnusson、Perry A. Frey

  DOI：10.1021/ja0013780

  日期：2000.9.1

  The question of how coenzyme B-12-dependent enzymes facilitate the cleavage of the Co-C bond of the cofactor is of interest. We have synthesized an analogue of 5'-deoxyadenosylcobalamin (AdoCbl(1)) designed to stabilize the 5'-deoxyadenosyl radical (5'-deoxyadenosine-5'-yl) that is produced upon homolysis of the Co-C bond. By replacement of the upper axial ligand of AdoCbl by a 3',4'-anhydro-5'-deoxyadenosyl moiety, the radical formed on the nucleoside analogue is stabilized by allylic delocalization. The compound, 5'-deoxy- 3',4'-anhydroadenosylcobalamin (3',4'-anAdoCbl) was synthesized by chemical and enzymatic methods. The final step was coupling of cob(I)alamin and 3',4'-anhydroATP catalyzed by CobA, an ATP: corrinoid adenosyltransferase. 3',4'-anAdoCbl displays interesting properties. The compound has not been purified to homogeneity due to its thermal and oxygen sensitivity. It was characterized by UV-vis spectroscopy, ESI-MS, and NMR spectroscopy. The bond dissociation energy of the Co-C bond of the analogue was measured by radical trapping techniques. A significantly weaker bond (24 +/- 2 kcal/mol) as compared to AdoCbl (30 kcal/mol) was observed, as was homolytic cleavage at ambient temperature. Photolysis experiments conducted under anaereobic conditions reveal no formation of cob(II)alamin, whereas the compound breaks down rapidly under aerobic conditions as measured by cob(In)alamin formation. We postulate that the weak Co-C bond is cleaved reversibly by photolysis, where recombination of the allylic radical and cob(II)alamin occurs efficiently in the absence of a radical scavanger. Activation of the coenzyme Bit-dependent enzymes diol dehydrase and ethanolamine ammonia-lyase was observed with the cofactor analogue. The measured activity was low and no formation of cob(II)alamin could be detected in the steady-state of the reaction for either enzyme. Comparative interactions of AdoCbl and 3',4'-anAdoCbl with diol dehydrase and ethanolamine ammonia-lyase suggest that cleavage of the Co-C bond is facilitated by enzyme-coenzyme binding contacts that are remote from the Co-C bond.