Z-Glu(α-OtBu)-γ-Glu(α-OtBu)(γ-OTMSE) | 357958-53-3

• 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: Z-Glu(α-OtBu)-γ-Glu(α-OtBu)(γ-OTMSE)
• 英文别名: Cbz-gGlu(OtBu)-Glu(OEtTMS)-OtBu；1-O-tert-butyl 5-O-(2-trimethylsilylethyl) (2S)-2-[[(4S)-5-[(2-methylpropan-2-yl)oxy]-5-oxo-4-(phenylmethoxycarbonylamino)pentanoyl]amino]pentanedioate
• CAS: 357958-53-3
• 化学式: C₃₁H₅₀N₂O₉Si
• 分子量: 622.831
• InChiKey: BUIWUIFZNHVUSI-ZEQRLZLVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.89
• 重原子数：
  43
• 可旋转键数：
  21
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.65
• 拓扑面积：
  146
• 氢给体数：
  2
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  Z-Glu(α-OtBu)-γ-Glu(α-OtBu)(γ-OTMSE) 在 palladium on activated charcoal 4-二甲氨基吡啶 、 四丁基氟化铵 、 氢气 、 1-羟基苯并三唑 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 、 三氟乙酸 作用下， 以 四氢呋喃 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 生成 (S)-4-[(S)-1-Carboxy-2-(4-hydroxy-3-nitro-phenyl)-ethylcarbamoyl]-2-[(S)-4-carboxy-4-(4-methylamino-benzoylamino)-butyrylamino]-butyric acid
  参考文献：
  名称：

  N-Me-pAB-Glu-γ-Glu-γ-Tyr(3-NO2): an internally quenched fluorogenic γ-glutamyl hydrolase substrate

  摘要：

  A gamma -glutamyl tripeptide containing an internally quenched fluorophore has been synthesized and shown to be a substrate for recombinant rat gamma -glutamyl hydrolase. HPLC, LC-MS, and fluorescence spectra support the conclusion that selective hydrolysis occurs at the penultimate peptide bond. Preliminary data indicate that hydrolysis of this substrate can be monitored continuously to yield steady-state kinetic data (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(01)00103-2
• 作为产物：
  描述：

  (S)-2-Benzyloxycarbonylamino-pentanedioic acid 5-(2-trimethylsilanyl-ethyl) ester 在 palladium on activated charcoal 4-二甲氨基吡啶 、 氢气 、 氢气 、 1-羟基苯并三唑 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 Z-Glu(α-OtBu)-γ-Glu(α-OtBu)(γ-OTMSE)
  参考文献：
  名称：

  N-Me-pAB-Glu-γ-Glu-γ-Tyr(3-NO2): an internally quenched fluorogenic γ-glutamyl hydrolase substrate

  摘要：

  A gamma -glutamyl tripeptide containing an internally quenched fluorophore has been synthesized and shown to be a substrate for recombinant rat gamma -glutamyl hydrolase. HPLC, LC-MS, and fluorescence spectra support the conclusion that selective hydrolysis occurs at the penultimate peptide bond. Preliminary data indicate that hydrolysis of this substrate can be monitored continuously to yield steady-state kinetic data (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(01)00103-2

文献信息

• N-Me-pAB-Glu-γ-Glu-γ-Tyr(3-NO2): an internally quenched fluorogenic γ-glutamyl hydrolase substrate
  作者：Jessica J. Pankuch、James K. Coward

  DOI：10.1016/s0960-894x(01)00103-2

  日期：2001.6

  A gamma -glutamyl tripeptide containing an internally quenched fluorophore has been synthesized and shown to be a substrate for recombinant rat gamma -glutamyl hydrolase. HPLC, LC-MS, and fluorescence spectra support the conclusion that selective hydrolysis occurs at the penultimate peptide bond. Preliminary data indicate that hydrolysis of this substrate can be monitored continuously to yield steady-state kinetic data (C) 2001 Elsevier Science Ltd. All rights reserved.