BZ-DL-Arg-OH hcl | 125652-40-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: BZ-DL-Arg-OH hcl
• 英文别名: 2-benzamido-5-(diaminomethylideneamino)pentanoic acid;hydrochloride
• CAS: 125652-40-6
• 化学式: C₁₃H₁₈N₄O₃*ClH
• 分子量: 314.772
• InChiKey: LSLUHKRVLRTIBV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.35
• 重原子数：
  21
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  131
• 氢给体数：
  5
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  BZ-DL-Arg-OH hcl 、 苯胺 生成 N^α-Benzoyl-DL-arginin-anilid
  参考文献：
  名称：

  色氨酸精氨酸衍生物作为胰蛋白酶的基质的合成。

  摘要：

  DOI：

  10.1021/jo01017a017
• 作为产物：
  描述：

  N-苯甲酰基-DL-精氨酰-4-硝基苯胺盐酸盐 在 水 、 papain 作用下， 以 四氢呋喃 为溶剂， 生成 BZ-DL-Arg-OH hcl 、 4-硝基苯胺
  参考文献：
  名称：

  Photoregulation of papain activity through anchoring photochromic azo groups to the enzyme backbone

  摘要：

  The enzyme papain has been chemically modified by 4-carboxyazobenzene (1), 3-carboxyazobenzene, (2), and 2-carboxyazobenzene, (3). The activities of the modified enzymes relative to native papain and the extent of loading by the azobenzene groups have been determined. trans-1-papain exhibits reversible photochromic properties, and upon illumination (lambda = 320 nm), interconversion to cis-1-papain occurs. Further illumination of cis-1-papain (lambda > 400 nm) regenerates trans-1-papain. The biocatalyst trans-1-papain is 2.75-fold more active than cis-1-papain toward hydrolysis of N-alpha-benzoyl-DL-arginine-4-nitroanilide (BAPNA; 4). The difference in activities of the trans/cis photochromic enzyme allows photoregulation of the hydrolytic process. Kinetic analyses reveal that the difference in activities of the two photochromic forms of 1-papain originates from poorer binding properties of cis-1-papain toward the substrate, as compared to trans-1-papain. The biocatalyst trans-1-papain is immobilized into Alginate beads, and cyclic photoregulated hydrolysis of BAPNA is effected.

  DOI：

  10.1021/ja00009a016

文献信息

• Synthesis of Chromogenic Arginine Derivatives as Substrates for Trypsin^*,1
  作者：Robert E. Plapinger、Marvin M. Nachlas、Myron L. Seligman、Arnold M. Seligman

  DOI：10.1021/jo01017a017

  日期：1965.6
• Photoregulation of papain activity through anchoring photochromic azo groups to the enzyme backbone
  作者：Itamar Willner、Shai Rubin、Azalia Riklin

  DOI：10.1021/ja00009a016

  日期：1991.4

  The enzyme papain has been chemically modified by 4-carboxyazobenzene (1), 3-carboxyazobenzene, (2), and 2-carboxyazobenzene, (3). The activities of the modified enzymes relative to native papain and the extent of loading by the azobenzene groups have been determined. trans-1-papain exhibits reversible photochromic properties, and upon illumination (lambda = 320 nm), interconversion to cis-1-papain occurs. Further illumination of cis-1-papain (lambda > 400 nm) regenerates trans-1-papain. The biocatalyst trans-1-papain is 2.75-fold more active than cis-1-papain toward hydrolysis of N-alpha-benzoyl-DL-arginine-4-nitroanilide (BAPNA; 4). The difference in activities of the trans/cis photochromic enzyme allows photoregulation of the hydrolytic process. Kinetic analyses reveal that the difference in activities of the two photochromic forms of 1-papain originates from poorer binding properties of cis-1-papain toward the substrate, as compared to trans-1-papain. The biocatalyst trans-1-papain is immobilized into Alginate beads, and cyclic photoregulated hydrolysis of BAPNA is effected.