Ac-D-Phe-D-Phe | 24809-16-3

• 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: Ac-D-Phe-D-Phe
• 英文别名: Ac-D-F-D-F；N-acetylphenylalanyl-phenylalanine；(2R)-2-[[(2R)-2-acetamido-3-phenylpropanoyl]amino]-3-phenylpropanoic acid
• CAS: 24809-16-3
• 化学式: C₂₀H₂₂N₂O₄
• 分子量: 354.406
• InChiKey: RXVJYWBNKIQSSP-QZTJIDSGSA-N

物化性质

• 沸点：
  692.3±55.0 °C(Predicted)
• 密度：
  1.225±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.9
• 重原子数：
  26
• 可旋转键数：
  8
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  95.5
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  Ac-D-Phe-D-Phe 、 2-溴乙酸苄酯 在 potassium carbonate 作用下， 以 丙酮 为溶剂， 反应 24.0h， 以84%的产率得到benzyl-O-(N-acetyl-phenylalanyl-phenylalanyl)-glycolate
  参考文献：
  名称：

  [EN] ENZYME INHIBITORS
  [FR] INHIBITEURS D'ENZYMES

  摘要：

  式（I）的化合物中，其中R是C-末端酰胺生物分子的生物分子残基或其衍生物，通过PAM的作用被激活；X是O或CH2或其盐或前药。

  公开号：

  WO2004007417A1
• 作为产物：
  描述：

  (Z)-(2-乙酰氨基-3-苯基丙烯酰基)-L-苯丙氨酸 在 Rh^I 氢气 作用下， 以 乙醇 为溶剂， 反应 0.25h， 生成 Ac-D-Phe-D-Phe
  参考文献：
  名称：

  Yamagishi, Takamichi; Ikeda, Satoru; Yatagai, Masanobu, Journal of the Chemical Society. Perkin transactions I, 1988, p. 1787 - 1790

  摘要：

  DOI：

文献信息

• Asymmetric Hydrogenation of Dehydrodipeptides with Rhodium(I)–Chiral Diphosphinites. Selective (<i>S</i>,<i>S</i>)- and (<i>R</i>,<i>R</i>)-Product Formation by Double Asymmetric Induction
  作者：Masanobu Yatagai、Takamichi Yamagishi、Mitsuhiko Hida

  DOI：10.1246/bcsj.57.823

  日期：1984.3

  stereoselectivities, depending on the chiral center of the substrates. This result was ascribed to the electrostatic interaction between the ligand and substrate. POP’s without ω-(dimethylamino)alkyl group gave (R,R)-product for (R)-substrate in a high stereoselectivity by the steric effect between the ligand and substrate, while for (S)-substrate, (S,S)-product was obtained in a low stereoselectivity.

  在脱氢二肽的氢化中，使用含有吡咯烷部分的 Rh(I)-手性二亚膦酸盐 (POP) 的催化剂检查了底物 ((S) 或 (R)) 的手性中心对不对称诱导的影响。具有 ω-(二甲氨基) 烷基的 POP 的催化剂显示出极大的双不对称诱导，以高立体选择性产生 (S,S)- 或 (R,R)- 产物，具体取决于底物的手性中心。该结果归因于配体和底物之间的静电相互作用。没有ω-（二甲氨基）烷基的POPs通过配体和底物之间的空间效应以高立体选择性为（R）-底物提供（R，R）-产物，而对于（S）-底物，（S，S） -产物以低立体选择性获得。
• Aminolytic reaction catalyzed by d-stereospecific amidohydrolases from Streptomyces spp
  作者：Jiro Arima、Hitomi Ito、Tadashi Hatanaka、Nobuhiro Mori

  DOI：10.1016/j.biochi.2011.04.020

  日期：2011.9

  From investigation of 2000 soil isolates, we identified two serine-type amidohydrolases that can hydrolyze D-aminoacyl derivatives from the culture supernatant of Streptomyces species 82F2 and 83D12. The enzymes, redesignated as 82F2-DAP and 83D12-DAP, were purified for homogeneity and characterized. Each enzyme had molecular mass of approximately 40 kDa, and each showed moderate stability with respect to temperature and pH. Among hydrolytic activities toward D-aminoacyl-pNAs, the enzymes showed strict specificity toward D-Phe-pNA, but showed broad specificity toward D-aminoacyl esters. The specific activity for D-Phe-pNA hydrolysis of 82F2-DAP was ten-fold higher than that of 83D12-DAP. As a second function, each enzyme showed peptide bond formation activity by its function of aminolysis reaction. Based on results of D-Phe D-Phe synthesis under various conditions, we propose a reaction mechanism for D-Phe D-Phe production. Furthermore, the enzymes exhibited peptide elongation activity, producing oligo homopeptide in a one-pot reaction. We cloned the genes encoding each enzyme, which revealed that the primary structure of each enzyme showed 30-60% identity with those of peptidases belonging to the clan SE, S12 peptidase family categorized as serine peptidase with D-stereospecificity. (C) 2011 Elsevier Masson SAS. All rights reserved.
• YAMAGISHI, TAKAMICHI;IKEDA, SATORU;YATAGAI, MASANOBU;YAMAGUCHI, MOTOWO;HI+, J. CHEM. SOC. PERKIN TRANS. PT 1,(1988) N 7, C. 1787-1790
  作者：YAMAGISHI, TAKAMICHI、IKEDA, SATORU、YATAGAI, MASANOBU、YAMAGUCHI, MOTOWO、HI+

  DOI：——

  日期：——