5'-O-(N-lysinylsulfamoyl)adenosine | 713543-21-6

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷
• 英文名称: 5'-O-(N-lysinylsulfamoyl)adenosine
• 英文别名: (1Z,2S)-6-amino-N-[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxysulfonyl]-2-azaniumylhexanimidate
• CAS: 713543-21-6
• 化学式: C₁₆H₂₆N₈O₇S
• 分子量: 474.498
• InChiKey: NARKTLKJPPMFJF-LEJQEAHTSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.6
• 重原子数：
  32
• 可旋转键数：
  10
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  252
• 氢给体数：
  6
• 氢受体数：
  13

反应信息

• 作为产物：
  描述：

  6-N-benzyloxycarbonyl-2',3'-O-benzylidene-5'-O-[N-(N-Cbz-L-lysinyl(ε-Cbz))sulfamoyl]adenosine 在 palladium 10% on activated carbon 、 氢气 作用下， 以 水 、 异丙醇 为溶剂， 70.0 ℃ 、5.0 MPa 条件下， 反应 2.0h， 以36%的产率得到5'-O-(N-lysinylsulfamoyl)adenosine
  参考文献：
  名称：

  Investigation, optimization and synthesis of sulfamoyloxy-linked aminoacyl-AMP analogues

  摘要：

  Aminoacyl-tRNA synthetases (aaRSs) constitute a family of enzymes that transfer amino acids to their corresponding tRNA molecules to form aminoacyl-tRNAs and have been validated as potential drug targets. Sulfamoyloxy-linked aminoacyl-AMP analogues are potent inhibitors of aaRSs. In this article, we report the synthesis of several new sulfamoyl analogues of as-AMP that up to now have been difficult or even impossible to prepare with current synthetic strategies. The developed synthetic strategy relies on performing the synthesis under neutral conditions followed by global deprotection using catalytic hydrogenation affording the desired 5'-0-(N-aminoacyl)sulfamoyladenosine compounds. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2011.12.011

文献信息

• Process for producing functional non-naturally occurring proteins, and method for site-specific modification and immobilization of the proteins
  申请人：Kiga Daisuke

  公开号：US20090011459A1

  公开（公告）日：2009-01-08

  There is provided a process for industrial production of non-naturally occurring proteins composed of less than 20 amino acids, wherein the proteins retain their original functions while being capable of site-specific modification or immobilization, or having new functions not found in nature in addition to the original functions of the proteins. Specifically there are provided a process for producing a functional non-naturally occurring protein having a specific amino acid type(s) replaced with a natural amino acid(s) other than the amino acid type(s), the process comprising: a) matching a nucleic acid portion having a nucleotide sequence reflecting the genotype with a protein portion that is the translation product of the nucleic acid portion; b) selecting the matched molecule obtained in step a); c) introducing mutation into the nucleic acid portion of the matched molecule obtained in step b); d) amplifying the nucleic acid portion obtained in step c); e) providing the nucleic acid portion obtained in step d) to step a), to match the nucleic acid portion with a protein portion that is the translation product of the nucleic acid portion; and f) selecting the matched molecule obtained in step e), to produce a functional non-naturally occurring protein; and a method for site-specific modification and site-immobilization of a functional non-naturally occurring protein.
• US8227209B2
  申请人：——

  公开号：US8227209B2

  公开（公告）日：2012-07-24
• Investigation, optimization and synthesis of sulfamoyloxy-linked aminoacyl-AMP analogues
  作者：Itedale Namro Redwan、Thomas Ljungdahl、Morten Grøtli

  DOI：10.1016/j.tet.2011.12.011

  日期：2012.2

  Aminoacyl-tRNA synthetases (aaRSs) constitute a family of enzymes that transfer amino acids to their corresponding tRNA molecules to form aminoacyl-tRNAs and have been validated as potential drug targets. Sulfamoyloxy-linked aminoacyl-AMP analogues are potent inhibitors of aaRSs. In this article, we report the synthesis of several new sulfamoyl analogues of as-AMP that up to now have been difficult or even impossible to prepare with current synthetic strategies. The developed synthetic strategy relies on performing the synthesis under neutral conditions followed by global deprotection using catalytic hydrogenation affording the desired 5'-0-(N-aminoacyl)sulfamoyladenosine compounds. (C) 2011 Elsevier Ltd. All rights reserved.