benzyloxycarbonyl-L-phenylalanyl-L-arginyl-(4-methyl-7-coumaryl)amide | 65147-22-0

• 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: benzyloxycarbonyl-L-phenylalanyl-L-arginyl-(4-methyl-7-coumaryl)amide
• 英文别名: Benzyloxycarbonyl-phenylalanylarginine-4-methylcoumaryl-7-amide；benzyl N-[(2S)-1-[[(2S)-5-(diaminomethylideneamino)-2-[(4-methyl-2-oxochromen-7-yl)amino]pentanoyl]amino]-1-oxo-3-phenylpropan-2-yl]carbamate
• CAS: 65147-22-0
• 化学式: C₃₃H₃₆N₆O₆
• 分子量: 612.685
• InChiKey: ZJHZQAYHEHUARV-SVBPBHIXSA-N

物化性质

• 密度：
  1.32±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  45
• 可旋转键数：
  14
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.24
• 拓扑面积：
  187
• 氢给体数：
  5
• 氢受体数：
  8

安全信息

• WGK Germany：
  3
• 危险性防范说明：
  P261,P264,P270,P271,P280,P301+P312,P302+P352,P304+P340,P305+P351+P338,P330,P332+P313,P337+P313,P362,P403+P233,P405,P501
• 危险性描述：
  H302,H315,H319,H335

制备方法与用途

生物活性

N-CBZ-Phe-Arg-AMC（Z-FR-AMC）是一种组织蛋白酶底物，可用于评估溶酶体组织蛋白酶的活性。

反应信息

• 作为反应物：
  描述：

  benzyloxycarbonyl-L-phenylalanyl-L-arginyl-(4-methyl-7-coumaryl)amide 在 acetate buffer 、 Hypophthalmichthys molitrix 、 silver carp muscle cathepsin L₁ 作用下， 反应 0.17h， 生成 、 7-氨基-4-甲基香豆素
  参考文献：
  名称：

  Purification and Characterization of Cathepsin L from the Muscle of Silver Carp (Hypophthalmichthys molitrix)

  摘要：

  Cathepsin L in silver carp musle was purified to 48.4-fold by acid-heat treatment and ammonium sulfate fractionation, followed by a series of chromatographic separations. The molecular mass of the purified enzyme was 30 kDa determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified enzyme was activated by dithiothreitol and cysteine while it was substantially inhibited by E-64 and insensitive to PMSF and pepstatin A, suggesting that the purified enzyme belongs to a family of cysteine proteinase. Consistent with this conclusion, Zn2+, Cu2+, Co2+, Ni2+, and Fe2+ could strongly inhibit the activity of this enzyme. The optimal pH and temperature were 5.0 and 55 degrees C, respectively. The enzyme catalyzed the hydrolysis of Z-Phe-Arg-MCA with a parameter of K m (8.27 AM) and K cat (28.7 s(-1)) but hardly hydrolyzed Z-Arg-Arg-MCA, Arg-MCA, and Boc-Val-Leu-Lys-MCA. The microstructure analysis by scanning electron microscopy showed that this proteinase is capable of destroying the network structure of silver carp surimi gels. The enzyme exhibited a higher hydrolytic activity on surimi protein at 65 degrees C than at 40 degrees C.

  DOI：

  10.1021/jf062038m

文献信息

• Purification and Characterization of Cathepsin L from the Muscle of Silver Carp (<i>Hypophthalmichthys molitrix</i>)
  作者：Huan Liu、Lijun Yin、Nan Zhang、Shuhong Li、Changwei Ma

  DOI：10.1021/jf062038m

  日期：2006.12.1

  Cathepsin L in silver carp musle was purified to 48.4-fold by acid-heat treatment and ammonium sulfate fractionation, followed by a series of chromatographic separations. The molecular mass of the purified enzyme was 30 kDa determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified enzyme was activated by dithiothreitol and cysteine while it was substantially inhibited by E-64 and insensitive to PMSF and pepstatin A, suggesting that the purified enzyme belongs to a family of cysteine proteinase. Consistent with this conclusion, Zn2+, Cu2+, Co2+, Ni2+, and Fe2+ could strongly inhibit the activity of this enzyme. The optimal pH and temperature were 5.0 and 55 degrees C, respectively. The enzyme catalyzed the hydrolysis of Z-Phe-Arg-MCA with a parameter of K m (8.27 AM) and K cat (28.7 s(-1)) but hardly hydrolyzed Z-Arg-Arg-MCA, Arg-MCA, and Boc-Val-Leu-Lys-MCA. The microstructure analysis by scanning electron microscopy showed that this proteinase is capable of destroying the network structure of silver carp surimi gels. The enzyme exhibited a higher hydrolytic activity on surimi protein at 65 degrees C than at 40 degrees C.