(S)-2-(4,5-Dimethoxy-2-nitro-benzyloxycarbonylamino)-3-(4-hydroxy-phenyl)-propionic acid cyanomethyl ester | 869318-01-4

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (S)-2-(4,5-Dimethoxy-2-nitro-benzyloxycarbonylamino)-3-(4-hydroxy-phenyl)-propionic acid cyanomethyl ester
• CAS: 869318-01-4
• 化学式: C₂₁H₂₁N₃O₉
• 分子量: 459.412
• InChiKey: ORYTXEYGIZEXSX-INIZCTEOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.22
• 重原子数：
  33.0
• 可旋转键数：
  10.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  170.25
• 氢给体数：
  2.0
• 氢受体数：
  10.0

反应信息

• 作为反应物：
  描述：

  (S)-2-(4,5-Dimethoxy-2-nitro-benzyloxycarbonylamino)-3-(4-hydroxy-phenyl)-propionic acid cyanomethyl ester 在 tetrafluoroboric acid 、 三氟化硼乙醚 、 三乙胺 作用下， 以 甲醇 、 乙醚 、 二氯甲烷 、 乙腈 为溶剂， 反应 25.0h， 生成
  参考文献：
  名称：

  Site-Specific Incorporation of Glycosylated Serine and Tyrosine Derivatives into Proteins

  摘要：

  Glycosylation of proteins can have a dramatic effect on their physical, chemical, and biological properties. Analogues of dihydrofolate reductase and firefly luciferase containing glycosylated amino acids at single, predetermined sites have been elaborated. Misacylated suppressor tRNAs activated with glycosylated serine and tyrosine derivatives were used for suppression of the nonsense codons in a cell-free protein biosynthesizing system, thereby permitting the preparation of the desired glycosylated proteins. In this fashion, it was possible to obtain proteins containing both mono- and diglycosylated amino acids, including glycosylated serine and tyrosine moieties. For the modified firefly luciferases, the effect of these substitutions on the wavelength of the light emitted by firefly luciferase was investigated. The maximum wavelength for mutants containing peracetylated glycosylated serine derivatives at position 284 showed a red shift in the emission spectra. For mutants containing glycosylated tyrosines, the red shift was observed only when the carbohydrate moiety was fully deacetylated.

  DOI：

  10.1021/ja067466n
• 作为产物：
  描述：

  L-酪氨酸 在 碳酸氢钠 、 三乙胺 作用下， 生成 (S)-2-(4,5-Dimethoxy-2-nitro-benzyloxycarbonylamino)-3-(4-hydroxy-phenyl)-propionic acid cyanomethyl ester
  参考文献：
  名称：

  Site-Specific Incorporation of Glycosylated Serine and Tyrosine Derivatives into Proteins

  摘要：

  Glycosylation of proteins can have a dramatic effect on their physical, chemical, and biological properties. Analogues of dihydrofolate reductase and firefly luciferase containing glycosylated amino acids at single, predetermined sites have been elaborated. Misacylated suppressor tRNAs activated with glycosylated serine and tyrosine derivatives were used for suppression of the nonsense codons in a cell-free protein biosynthesizing system, thereby permitting the preparation of the desired glycosylated proteins. In this fashion, it was possible to obtain proteins containing both mono- and diglycosylated amino acids, including glycosylated serine and tyrosine moieties. For the modified firefly luciferases, the effect of these substitutions on the wavelength of the light emitted by firefly luciferase was investigated. The maximum wavelength for mutants containing peracetylated glycosylated serine derivatives at position 284 showed a red shift in the emission spectra. For mutants containing glycosylated tyrosines, the red shift was observed only when the carbohydrate moiety was fully deacetylated.

  DOI：

  10.1021/ja067466n

文献信息

• Analogues of Vaccinia Virus DNA Topoisomerase I Modified at the Active Site Tyrosine
  作者：Rong Gao、Yi Zhang、Ambar K. Choudhury、Larisa M. Dedkova、Sidney M. Hecht

  DOI：10.1021/ja044182z

  日期：2005.3.1

  The mechanism of type IB topoisomerase-mediated DNA relaxation was studied by modification of vaccinia topoisomerase I at the active site tyrosine (position 274) with several tyrosine analogues. These analogues had varied steric, electronic, and stereochemical features to permit assessment of those structural elements required to support topoisomerase function. Eleven tyrosine analogues were successfully incorporated into the active site of vaccinia topoisomerase I. It was found that only tyrosine analogues having the phenolic -OH group in the normal position relative to the protein backbone were active, Modifications that replaced the nucleophilic tyrosine OH (pK(a) approximate to 10.0) group with NH2 (pK(a) 4.6), SH (pK(a) approximate to 7.0), or I groups or that changed the orientation of the nucleophilic OH group essentially eliminated topoisomerase I function. For the active analogues, the electronic effects and H-bonding characteristics of substituents in the meta-position of the aromatic ring may be important in modulating topoisomerase I function. The pH profile for the functional analogues revealed a small shift toward lower pH when compared with wild-type topoisomerase I.