(alphaR)-alpha-氨基-N-(4-硝基苯基)-苯丙酰胺 | 14235-18-8

• 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
• 中文名称: (alphaR)-alpha-氨基-N-(4-硝基苯基)-苯丙酰胺
• 英文名称: H-D-Phe-pNA
• 英文别名: D-Phe-pNA；(2R)-2-amino-N-(4-nitrophenyl)-3-phenylpropanamide
• CAS: 14235-18-8
• 化学式: C₁₅H₁₅N₃O₃
• 分子量: 285.302
• InChiKey: GJHIOWXZFDVUKQ-CQSZACIVSA-N

物化性质

• 熔点：
  156.5-157.5 °C
• 沸点：
  543.0±50.0 °C(Predicted)
• 密度：
  1.323±0.06 g/cm3(Predicted)
• 溶解度：
  溶于氯仿、二氯甲烷、乙酸乙酯、DMSO、丙酮等。

计算性质

• 辛醇/水分配系数(LogP)：
  2
• 重原子数：
  21
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.13
• 拓扑面积：
  101
• 氢给体数：
  2
• 氢受体数：
  4

安全信息

• 海关编码：
  2924299090
• 储存条件：
  存储条件：2-8°C，干燥

反应信息

• 作为反应物：
  描述：

  (alphaR)-alpha-氨基-N-(4-硝基苯基)-苯丙酰胺 在 Streptomyces spp. 82F₂ D-aminopeptidase 作用下， 以 二甲基亚砜 为溶剂， 反应 0.08h， 生成 D-苯丙氨酸
  参考文献：
  名称：

  Aminolytic reaction catalyzed by d-stereospecific amidohydrolases from Streptomyces spp

  摘要：

  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.

  DOI：

  10.1016/j.biochi.2011.04.020
• 作为产物：
  描述：

  N-苄氧羰基-D-苯丙氨酸 在 氢溴酸 、 溶剂黄146 作用下， 生成 (alphaR)-alpha-氨基-N-(4-硝基苯基)-苯丙酰胺
  参考文献：
  名称：

  Inhibition of .ALPHA.-chymotrypsin by Suc-L-Tyr-D-Leu-D-Phe-pNA, a stereoisomer of a specific substrate.

  摘要：

  采用传统的溶液法合成了多种酶的特定发色底物的立体异构体。其中，Suc-L-Tyr-D-Leu-D-Phe-pNA 是一种有效的α-糜蛋白酶特异性抑制剂。然而，Suc-L-Tyr-D-Leu-D-Phe-Pipe 对α-糜蛋白酶没有任何抑制作用。对上述立体异构体中 pNA 分子的作用进行了研究，发现 pNA 分子参与了与酶的某些部分的结合，从而导致抑制活性的显现。

  DOI：

  10.1248/cpb.33.5301

文献信息

• Small molecules for treatment of hypercholesterolemia and related diseases
  申请人：Sircar C. Jagadish

  公开号：US20050277690A1

  公开（公告）日：2005-12-15

  The present invention provides compositions adapted to enhance reverse cholesterol transport in mammals. The compositions are suitable for oral delivery and useful in the treatment and/or prevention of hypercholesterolemia, atherosclerosis and associated cardiovascular diseases.

  本发明提供了适用于增强哺乳动物体内逆向胆固醇转运的组合物。这些组合物适合口服给药，并可用于治疗和/或预防高胆固醇血症、动脉粥样硬化及相关心血管疾病。
• 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.
• Inhibition of .ALPHA.-chymotrypsin by Suc-L-Tyr-D-Leu-D-Phe-pNA, a stereoisomer of a specific substrate.
  作者：YOSHIO OKADA、YUKO TSUDA、NAOKI TENO、YOKO NAGAMATSU、UTAKO OKAMOTO、NORIO NISHI

  DOI：10.1248/cpb.33.5301

  日期：——

  Stereoisomers of specific chromogenic substrates for various enzymes were synthesized by a conventional solution method. Among them, Suc-L-Tyr-D-Leu-D-Phe-pNA was found to be an effective and specific inhibitor of α-chymotrypsin. However, Suc-L-Tyr-D-Leu-D-Phe-Pipe did not show any inhibitory effect on α-chymotrypsin. The role of the pNA moiety of the above stereoisomer was investigated, and it was found that the pNA moiety participated in binding with some part of the enzyme, resulting in the manifestation of the inhibitory activity.

  采用传统的溶液法合成了多种酶的特定发色底物的立体异构体。其中，Suc-L-Tyr-D-Leu-D-Phe-pNA 是一种有效的α-糜蛋白酶特异性抑制剂。然而，Suc-L-Tyr-D-Leu-D-Phe-Pipe 对α-糜蛋白酶没有任何抑制作用。对上述立体异构体中 pNA 分子的作用进行了研究，发现 pNA 分子参与了与酶的某些部分的结合，从而导致抑制活性的显现。