tert-butyl (2S)-5-hydroxy-2-(N-(9-(9-phenylfluorenyl))amino)pentanoate | 119595-84-5

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: tert-butyl (2S)-5-hydroxy-2-(N-(9-(9-phenylfluorenyl))amino)pentanoate
• 英文别名: tert-butyl (S)-5-hydroxy-2-(N-(9-(9-phenylfluorenyl))amino)pentanoate；tert-butyl (2S)-5-hydroxy-2-{N-[9-(9-phenylfluorenyl)]amino}pentanoate；tert-butyl (2S)-5-hydroxy-2-[(9-phenylfluoren-9-yl)amino]pentanoate
• CAS: 119595-84-5
• 化学式: C₂₈H₃₁NO₃
• 分子量: 429.559
• InChiKey: GYXGQNQDUDVOAD-VWLOTQADSA-N

物化性质

• 熔点：
  123 °C(Solv: ethyl ether (60-29-7))
• 沸点：
  571.1±50.0 °C(Predicted)
• 密度：
  1.18±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  5.1
• 重原子数：
  32
• 可旋转键数：
  9
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.32
• 拓扑面积：
  58.6
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  tert-butyl (2S)-5-hydroxy-2-(N-(9-(9-phenylfluorenyl))amino)pentanoate 在 三氟乙酸 、 Dowex-50W resin [H(+)-form] 作用下， 以 二氯甲烷 、 水 为溶剂， 以91%的产率得到2-氨基-5-羟基-戊酸
  参考文献：
  名称：

  Biosynthesis of 4-Methylproline in Cyanobacteria:  Cloning of nosE and nosF Genes and Biochemical Characterization of the Encoded Dehydrogenase and Reductase Activities

  摘要：

  The biosynthesis of the unusual amino acid 4-methylproline in the Nostoc genus of cyanobacteria was investigated on the genetic and enzymatic level. Two genes involved in the biosynthesis were cloned and the corresponding enzymes, a zinc-dependent long-chain dehydrogenase and a Delta(1)-pyrroline-5-carboxylic acid (P5C) reductase homologue, were overexpressed in Escherichia coli and biochemically characterized. Putative substrates were synthesized to test enzyme substrate specificities, and deuterium labeling studies were carried out to reveal the stereospecificities of the enzymatic reactions with respect to the substrates as well as to the coenzymes.

  DOI：

  10.1021/jo026479q
• 作为产物：
  描述：

  L-谷氨酸-5-甲酯 在 lithium aluminium tetrahydride 、 lead(II) nitrate 、 碘乙腈 、 双(三甲基硅烷基)氨基钾 、 三乙胺 作用下， 以 四氢呋喃 、 二氯甲烷 、 氯仿 为溶剂， 反应 109.75h， 生成 tert-butyl (2S)-5-hydroxy-2-(N-(9-(9-phenylfluorenyl))amino)pentanoate
  参考文献：
  名称：

  Synthesis of 4-substituted prolines as conformationally constrained amino acid analogs

  摘要：

  DOI：

  10.1021/jo00269a022

文献信息

• KOSKINEN, ARI M. P.;RAPOPORT, HENRY, J. ORG. CHEM., 54,(1989) N, C. 1859-1866
  作者：KOSKINEN, ARI M. P.、RAPOPORT, HENRY

  DOI：——

  日期：——
• Synthesis of 4-substituted prolines as conformationally constrained amino acid analogs
  作者：Ari M. P. Koskinen、Henry Rapoport

  DOI：10.1021/jo00269a022

  日期：1989.4
• Biosynthesis of 4-Methylproline in Cyanobacteria:  Cloning of <i>n</i><i>osE</i> and <i>n</i><i>osF</i> Genes and Biochemical Characterization of the Encoded Dehydrogenase and Reductase Activities
  作者：Hendrik Luesch、Dietmar Hoffmann、Joan M. Hevel、Julia E. Becker、Trimurtulu Golakoti、Richard E. Moore

  DOI：10.1021/jo026479q

  日期：2003.1.1

  The biosynthesis of the unusual amino acid 4-methylproline in the Nostoc genus of cyanobacteria was investigated on the genetic and enzymatic level. Two genes involved in the biosynthesis were cloned and the corresponding enzymes, a zinc-dependent long-chain dehydrogenase and a Delta(1)-pyrroline-5-carboxylic acid (P5C) reductase homologue, were overexpressed in Escherichia coli and biochemically characterized. Putative substrates were synthesized to test enzyme substrate specificities, and deuterium labeling studies were carried out to reveal the stereospecificities of the enzymatic reactions with respect to the substrates as well as to the coenzymes.