N-[9-((3aR,4R,6R,6aR)-2,2-Dimethyl-6-(S)-oxiranyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-yl)-9H-purin-6-yl]-benzamide | 104409-53-2

• 分子结构分类: 有机化合物 - 有机杂环化合物
• 英文名称: N-[9-((3aR,4R,6R,6aR)-2,2-Dimethyl-6-(S)-oxiranyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-yl)-9H-purin-6-yl]-benzamide
• CAS: 104409-53-2
• 化学式: C₂₁H₂₁N₅O₅
• 分子量: 423.428
• InChiKey: ZLCGSUJJHZDCEN-AFFICDNSSA-N

反应信息

• 作为反应物：
  描述：

  N-[9-((3aR,4R,6R,6aR)-2,2-Dimethyl-6-(S)-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， 生成 N-[9-((3aR,4R,6S,6aS)-2,2-Dimethyl-6-(S)-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
• 作为产物：
  描述：

  N-{9-[(2R,3R,4S,5R)-5-((R)-1,2-Dihydroxy-ethyl)-3,4-dihydroxy-tetrahydro-furan-2-yl]-9H-purin-6-yl}-benzamide 在 吡啶 、 咪唑 、 四丁基氟化铵 、 APTS 作用下， 以 四氢呋喃 、 丙酮 为溶剂， 生成 N-[9-((3aR,4R,6R,6aR)-2,2-Dimethyl-6-(S)-oxiranyl-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