Boc-Leu-Lys-Arg-AMC | 109358-47-6

• 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: Boc-Leu-Lys-Arg-AMC
• 英文别名: Boc-Leu-Lys-Arg-MCA；Boc-leu-lys-arg-amc hydrochloride salt；tert-butyl N-[(2S)-1-[[(2S)-6-amino-1-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]carbamate
• CAS: 109358-47-6
• 化学式: C₃₃H₅₂N₈O₇
• 分子量: 672.825
• InChiKey: RRHPIUJOSIJECH-SDHOMARFSA-N

物化性质

• 密度：
  1.29±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  48
• 可旋转键数：
  19
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  242
• 氢给体数：
  7
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  Boc-Leu-Lys-Arg-AMC 在 2-吗啉乙磺酸 APC-8754 、 sodium acetate 、 human liver cathepsin B 作用下， 以 水 、 二甲基亚砜 为溶剂， 生成 7-氨基-4-甲基香豆素
  参考文献：
  名称：

  靶向组织蛋白酶B封闭环的抑制剂的pH依赖性。

  摘要：

  以前已经基于天然产物半胱氨酸蛋白酶抑制剂E-64合成了强力和选择性组织蛋白酶B抑制剂。X射线晶体数据表明，这些化合物通过其游离羧酸盐与位于组织蛋白酶B闭塞环内活性位点主端的带正电荷的组氨酸残基相互作用。在此，我们研究了两个主端的pH依赖性结合化合物。在每种情况下，随着pH从4升高到7.8（对应于pK（a）4.4的单个电离），k（inact）/ K（I）都会显着降低。这些结果表明，如果酶环境的pH值大于5.5，靶向组织蛋白酶B的闭环可能是不良的抑制剂设计策略。然而，

  DOI：

  10.1016/s0045-2068(02)00009-3

文献信息

• pH Dependence of inhibitors targeting the occluding loop of cathepsin B
  作者：Brian E Cathers、Cynthia Barrett、James T Palmer、Robert M Rydzewski

  DOI：10.1016/s0045-2068(02)00009-3

  日期：2002.8

  selective cathepsin B inhibitors have previously been synthesized based upon the natural product cysteine protease inhibitor E-64. X-ray crystal data indicates that these compounds interact through their free carboxylate with the positively charged histidine residues located on the prime-side of the active site within the occluding loop of cathepsin B. Herein, we examine the pH dependence of two prime-side-binding

  以前已经基于天然产物半胱氨酸蛋白酶抑制剂E-64合成了强力和选择性组织蛋白酶B抑制剂。X射线晶体数据表明，这些化合物通过其游离羧酸盐与位于组织蛋白酶B闭塞环内活性位点主端的带正电荷的组氨酸残基相互作用。在此，我们研究了两个主端的pH依赖性结合化合物。在每种情况下，随着pH从4升高到7.8（对应于pK（a）4.4的单个电离），k（inact）/ K（I）都会显着降低。这些结果表明，如果酶环境的pH值大于5.5，靶向组织蛋白酶B的闭环可能是不良的抑制剂设计策略。然而，
• Low molecular weight trypsin from hepatopancreas of freshwater prawn (Macrobrachium rosenbergii): Characteristics and biochemical properties
  作者：Chodsana Sriket、Soottawat Benjakul、Wonnop Visessanguan、Kenji Hara、Asami Yoshida、Xiao Liang

  DOI：10.1016/j.foodchem.2012.02.173

  日期：2012.9

  Trypsin was purified to homogeneity from hepatopancreas of freshwater prawn (HFWP) (Macrobrachium rosenbergii) using a series of chromatographies including Q-Sepharose, Superdex 75 and MonoQ columns. HFWP trypsin was purified 525-fold with a yield of 10.6%. Based on native-PAGE, the purified trypsin showed a single band. Trypsin had a molecular weight of 17 kDa as estimated by SDS-PAGE. The optimal pH and temperature for Boc-Val-Pro-Arg-MCA hydrolysis were 8.0 and 55 degrees C, respectively. Trypsin was stable to heat treatment up to 40 degrees C, and over a pH range of 7.0-11.0. Trypsin activity was strongly inhibited by soybean trypsin inhibitor, N-p-tosyl-L-lysine chloromethyl ketone (TLCK) and Pefabloc SC and was partially inhibited by ethylenediaminetetraacetic acid (EDTA). Apparent K-m value of trypsin was 0.24 mu M and K-cat value was 607.56 s(-1) for Boc-Val-Pro-Arg-MCA. The N-terminal amino acid sequence of 20 residues of HFWP trypsin was IVGGDEAAPGEFPHQISMQV, which was highly homologous with those from other species of prawn. HFWP trypsin also showed high collagenolytic activity toward prawn, shrimp and fish collagens, suggesting its possible role in muscle softening of freshwater prawn during extended storage. (C) 2012 Elsevier Ltd. All rights reserved.