N-[9-((3aR,4R,6S,6aS)-2,2-Dimethyl-6-(R)-thiiranyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-yl)-9H-purin-6-yl]-benzamide | 898221-44-8

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 咪唑并嘧啶类
• 英文名称: N-[9-((3aR,4R,6S,6aS)-2,2-Dimethyl-6-(R)-thiiranyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-yl)-9H-purin-6-yl]-benzamide
• CAS: 898221-44-8
• 化学式: C₂₁H₂₁N₅O₄S
• 分子量: 439.495
• InChiKey: TXSCLIMEHRSPPQ-AFFICDNSSA-N

反应信息

• 作为反应物：
  描述：

  N-[9-((3aR,4R,6S,6aS)-2,2-Dimethyl-6-(R)-thiiranyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-yl)-9H-purin-6-yl]-benzamide 在 sodium methylate 、 溶剂黄146 作用下， 以 甲醇 为溶剂， 反应 2.0h， 生成 (2R,3R,4S,5S)-2-(6-Amino-purin-9-yl)-5-(R)-thiiranyl-tetrahydro-furan-3,4-diol
  参考文献：
  名称：

  Inactivation of human S-adenosylhomocysteine hydrolase by covalent labeling of cysteine 195 with thionucleoside derivatives

  摘要：

  -A new series of 5'-thioadenosine derivatives 1-4 were synthesized for selectively targeting (CYS)-C-195 of human AdoHcy hydrolase. Their incubation with the enzyme resulted in time- and concentration-dependent inactivation, without major modifications of the NAD(+)/NADH ratio. The electrospray mass analysis of the inactivated enzyme with 1, 2, 3, and 4b showed that inhibition was accompanied by the formation of a specific and covalent labeling of each AdoHcy hdrolase subunit. Proteolytic cleavage (endo-Lys-C) and subsequent peptide characterization of the labeled enzyme revealed that (195)Cys was the residue modified during the inactivation process. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2004.09.051
• 作为产物：
  描述：

  N-[9-((3aR,4R,6R,6aR)-2,2-Dimethyl-6-(R)-oxiranyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-yl)-9H-purin-6-yl]-benzamide 在 硫脲 作用下， 以 甲醇 为溶剂， 以55%的产率得到N-[9-((3aR,4R,6S,6aS)-2,2-Dimethyl-6-(R)-thiiranyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-yl)-9H-purin-6-yl]-benzamide
  参考文献：
  名称：

  Inactivation of human S-adenosylhomocysteine hydrolase by covalent labeling of cysteine 195 with thionucleoside derivatives

  摘要：

  -A new series of 5'-thioadenosine derivatives 1-4 were synthesized for selectively targeting (CYS)-C-195 of human AdoHcy hydrolase. Their incubation with the enzyme resulted in time- and concentration-dependent inactivation, without major modifications of the NAD(+)/NADH ratio. The electrospray mass analysis of the inactivated enzyme with 1, 2, 3, and 4b showed that inhibition was accompanied by the formation of a specific and covalent labeling of each AdoHcy hdrolase subunit. Proteolytic cleavage (endo-Lys-C) and subsequent peptide characterization of the labeled enzyme revealed that (195)Cys was the residue modified during the inactivation process. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2004.09.051