N-[3-(2-呋喃基)-1-氧代-2-丙烯-1-基]-L-苯丙氨酸 | 71115-83-8

• 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: N-[3-(2-呋喃基)-1-氧代-2-丙烯-1-基]-L-苯丙氨酸
• 英文名称: N-<3-(2-furyl)acryloyl>-Phe
• 英文别名: N-(3-(2-furyl)acryloyl)phenylalanine；Fua-Phe-OH；Fua-Phe；FAPP；N-<3-<2>Furyl-acryloyl>-L-phenylalanin；N-(3-[2]Furyl-acryloyl)-L-phenylalanin；(2S)-2-[3-(furan-2-yl)prop-2-enamido]-3-phenylpropanoic acid；(2S)-2-[3-(furan-2-yl)prop-2-enoylamino]-3-phenylpropanoic acid
• CAS: 71115-83-8
• 化学式: C₁₆H₁₅NO₄
• 分子量: 285.299
• InChiKey: QSMRHXUZHXEHBK-AWEZNQCLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  21
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  79.5
• 氢给体数：
  2
• 氢受体数：
  4

安全信息

• 海关编码：
  2932190090

反应信息

• 作为反应物：
  描述：

  N-[3-(2-呋喃基)-1-氧代-2-丙烯-1-基]-L-苯丙氨酸 在 碳酸氢钠 、 N,N'-二环己基碳二亚胺 作用下， 以 1,4-二氧六环 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 22.0h， 生成 FA-Phe-Ile
  参考文献：
  名称：

  Characterization of the Substrate Specificity of Human Carboxypeptidase A4 and Implications for a Role in Extracellular Peptide Processing

  摘要：

  CPA4 (carboxypeptidase A4) is a member of the metallocarboxypeptidase family. CPA4 was originally found in a screen of mRNAs up-regulated by sodium butyrate-induced differentiation of cancer cells. Further studies suggested a relation between CPA4 and prostate cancer aggressiveness. In the present study, we determined that CPA4 is secreted from cells as a soluble proenzyme (pro-CPA4) that can be activated by endoproteases, such as trypsin. Three complementary approaches were used to study the substrate specificity of CPA4; kinetic analysis was performed using a new series of chromogenic substrates and some biologically relevant peptides, the cleavage of synthetic peptides was tested individually, and the cleavage of a mixture of > 100 mouse brain peptides was examined using a quantitative peptidomics mass spectrometry-based approach. CPA4 was able to cleave hydrophobic C-terminal residues with a preference for Phe, Leu, Ile, Met, Tyr, and Val. However, not all peptides with C-terminal hydrophobic residues were cleaved, indicating the importance of additional residues within the peptide. Aliphatic, aromatic, and basic residues in the P1 position have a positive influence on the cleavage specificity. In contrast, acidic residues, Pro, and Gly have a negative influence in the P1 position. Some of the peptides identified as CPA4 substrates (such as neurotensin, granins, and opioid peptides) have been previously shown to function in cell proliferation and differentiation, potentially explaining the link between CPA4 and cancer aggressiveness. Taken together, these studies suggest that CPA4 functions in neuropeptide processing and regulation in the extracellular environment.

  DOI：

  10.1074/jbc.m109.060350
• 作为产物：
  描述：

  N-<3-(2-furyl)acryloyl>phenylalanine ethyl ester 在 双甘肽 、 N,N-二甲基甲酰胺 作用下， 以100%的产率得到N-[3-(2-呋喃基)-1-氧代-2-丙烯-1-基]-L-苯丙氨酸
  参考文献：
  名称：

  Wheat Carboxypeptidase-Catalyzed Peptide Synthesis by Aminolysis ofN-Acyl Amino Acid Ester. Indication of the Acyl-Enzyme Mechanism

  摘要：

  研究了小麦麸皮羧肽酶（羧肽酶W）催化的N-[3-(2-呋喃)丙烯酰]-酰化（Fua-）氨基酸乙酯与氨基酸酰胺的二肽合成。最适pH为8，在最佳条件下，超过60%的初始N-Fua-L-苯丙氨酸乙酯转化为N-Fua-L-苯丙氨酰甘氨酰胺。二肽形成对氨基酸酰胺浓度的依赖性表现出明显的饱和现象；这种现象可以通过一个涉及酰化酶被酶结合胺攻击的反应方案成功解释。在存在两种不同胺组分的反应中，结果也支持这一机制。甘氨酰胺对酰化羧肽酶具有更好的亲和性，表观解离常数（KN(app)）约为50 mM。这些结果与酵母和麦芽来源的羧肽酶催化的反应进行了比较。

  DOI：

  10.1246/bcsj.60.1403

文献信息

• Protease-Catalyzed Peptide Formation under High Pressure
  作者：Shigeru Kunugi、Kazuo Tanabe、Kouji Yamashita、Yoshio Morikawa、Takanobu Ito、Toshihiro Kondoh、Kouichirou Hirata、Akihiko Nomura

  DOI：10.1246/bcsj.62.514

  日期：1989.2

  The effect of high pressure on peptide formation by the catalysis of carboxypeptidase Y (substitution of ester or peptide by amino acid derivative) or by thermolysin (condensation of N-acylamino acid and amino acid amide) was studied. The carboxypeptidase Y-catalyzed substitution reaction of N-[3-(2-furyl)acryloyl]phenylalanine ethyl ester with glycinamide or phenylalaninamide showed a six-fold higher

  研究了高压对羧肽酶 Y（酯或肽被氨基酸衍生物取代）或嗜热菌蛋白酶（N-酰基氨基酸和氨基酸酰胺的缩合）的催化作用对肽形成的影响。N-[3-(2-呋喃基)丙烯酰基]苯丙氨酸乙酯与甘氨酰胺或苯丙氨酰胺的羧肽酶Y催化的取代反应在200 MPa下显示出比在大气压下高六倍的总肽产率。在N-酰基肽和氨基酸酰胺反应的情况下，肽产率和取代效率在升高的压力下均得到改善，并且底物的浪费性水解通过升高的压力得到高度抑制。压力还可以有效地消除N-酰基氨基酸酯与氨基酸酯反应中氨基酸酯对底物的抑制作用，并在高压下产生大量的二肽酯。通过对嗜热菌蛋白酶反应的压力来提高肽产率是显而易见的。
• The effect of pressure on protease-catalysed peptide formation
  作者：S. Kunugi、K. Tanabe、M. Fukuda、S. Makimoto、Y. Taniguchi

  DOI：10.1039/c39870001335

  日期：——

  Peptide formation from an N-acyl amino acid ester and an amino acid amide using carboxypeptidase Y as a catalyst was shown to be considerably influenced by applying high pressure; at 150 MPa the peptide yield was almost five-fold higher than that at 0.1 MPa when PheNH2 was used as the nucleophile.

  由羧肽酶Y作为催化剂，由N-酰基氨基酸酯和氨基酸酰胺形成的肽显示出受高压的影响很大。当使用PheNH 2作为亲核试剂时，在150 MPa的条件下，肽的收率几乎是在0.1 MPa时的肽收率的五倍。
• Action of Serine Carboxypeptidases on Endopeptidase Substrates,<i>N</i>-Acyldipeptideamides
  作者：Shigeru Kunugi、Kazuo Tanabe、Kouji Yamashita、Mitsuhiro Fukuda

  DOI：10.1246/bcsj.60.1399

  日期：1987.4

  activity on these substrates. On the contrary, carboxypeptidase Y gave Fua-amino acids and Fua-dipeptides as products, depending on the structure of the substrates. Accordingly, liberations of free amino acids were detected in some cases. This result shows that the yeast enzyme acts on some of the substrates in a two step manner: First by amidase and second by a carboxypeptidase activity. Based on

  两种丝氨酸羧肽酶，一种来自酵母 (Y)，另一种来自麦麸 (W)，对 N-[3-(2-呋喃基) 丙烯酰基]-(Fua-) 二肽酰胺底物的作用模式通过 HPLC 和氨基酸检测分析。在小麦酶的反应中，底物被水解为 Fua-氨基酸，在 HPLC 上没有检测到足够量的 Fua-二肽在产物混合物中。通过氨基酸分析观察到很少或没有游离氨基酸。这表明小麦酶对这些底物表现出羧酰胺肽酶活性。相反，羧肽酶 Y 根据底物的结构，产生 Fua-氨基酸和 Fua-二肽作为产物。因此，在某些情况下检测到游离氨基酸的释放。该结果表明酵母酶以两步方式作用于某些底物：首先是酰胺酶，其次是羧肽酶活性。基于这些结果，讨论了这些酶的底物结合机制。
• Shalaby; Abd Al-Salam; Kalmouch, Egyptian Journal of Chemistry, 2013, vol. 56, # 5-6, p. 401 - 415
  作者：Shalaby、Abd Al-Salam、Kalmouch、El-Shihaby、Abdullah

  DOI：——

  日期：——
• Wheat Carboxypeptidase-Catalyzed Peptide Synthesis by Aminolysis of<i>N</i>-Acyl Amino Acid Ester. Indication of the Acyl-Enzyme Mechanism
  作者：Hiroshi Shima、Mitsuhiro Fukuda、Kazuo Tanabe、Takanobu Ito、Shigeru Kunugi

  DOI：10.1246/bcsj.60.1403

  日期：1987.4

  Dipeptide synthesis from N-[3-(2-furyl)acryloyl]-acylated (Fua-) amino acid ethyl ester and amino acid amide catalyzed by wheat bran carboxypeptidase (carboxypeptidase W) was studied. The optimum pH for peptide formation was at pH 8; more than 60% of the initial N-Fua-l-phenylalanine ethyl ester was converted to N-Fua-l-phenylalanylglycinamide under optimum conditions. The dependence of peptide formation on the concentration of amino acid amide showed an apparent saturation; this could be successfully explained by a reaction scheme which involved an acylated enzyme attacked by an enzyme-bound amine. The results for a reaction in the presence of two different amine components also supported this mechanism. Gly–NH2 had a better affinity to the acylated carboxypeptidase and the apparent dissociation constant (KN(app)) was about 50 mM. These results were compared with those for those reactions catalyzed by carboxypeptidases from yeast and malt.

  研究了小麦麸皮羧肽酶（羧肽酶W）催化的N-[3-(2-呋喃)丙烯酰]-酰化（Fua-）氨基酸乙酯与氨基酸酰胺的二肽合成。最适pH为8，在最佳条件下，超过60%的初始N-Fua-L-苯丙氨酸乙酯转化为N-Fua-L-苯丙氨酰甘氨酰胺。二肽形成对氨基酸酰胺浓度的依赖性表现出明显的饱和现象；这种现象可以通过一个涉及酰化酶被酶结合胺攻击的反应方案成功解释。在存在两种不同胺组分的反应中，结果也支持这一机制。甘氨酰胺对酰化羧肽酶具有更好的亲和性，表观解离常数（KN(app)）约为50 mM。这些结果与酵母和麦芽来源的羧肽酶催化的反应进行了比较。