Z-丙氨酸-丙氨酸-丙氨酸-pNA | 61043-33-2

• 物质功能分类: 生物 - 细胞培养 - 添加剂
• 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: Z-丙氨酸-丙氨酸-丙氨酸-pNA
• 英文名称: Z-Ala-Ala-Leu-pNA
• 英文别名: benzyl N-[(2S)-1-[[(2S)-1-[[(2S)-4-methyl-1-(4-nitroanilino)-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]carbamate
• CAS: 61043-33-2
• 化学式: C₂₆H₃₃N₅O₇
• mdl: MFCD00038759
• 分子量: 527.577
• InChiKey: QFSQXEZZCBIDKW-SPEDKVCISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  38
• 可旋转键数：
  12
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.384
• 拓扑面积：
  171
• 氢给体数：
  4
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  Z-丙氨酸-丙氨酸-丙氨酸-pNA 在 Tris-HCl buffer 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 N-benzyloxycarbonyl-alanyl-alanyl-leucine
  参考文献：
  名称：

  Native subtilisin Karlsberg and modified subtilisin 72 as effective catalysts of peptide bond formation in organic media

  摘要：

  The activity and stability of native subtilisin Karlsberg and subtilisin 72 and their complexes with sodium dodecyl sulfate (SDS) in organic solvents were studied. The kinetic constants of the hydrolysis of specific chromogenic peptide substrates Z-Ala-Ala-Leu-pNA and Glp-Ala-Ala-Leu-pNA by the subtilisins were determined. It was found that the subtilisin Karlsberg complex with SDS in anhydrous organic solvents is an effective catalyst of peptide synthesis with multifunctional amino acids in positions P-1 and P-1', (Glu, At-, and Asp) containing unprotected side ionogenic groups.

  DOI：

  10.1134/s1068162006020026
• 作为产物：
  描述：

  N-(苄氧羰基)-L-丙氨酰-L-丙氨酸 、 L-亮氨酸-4-硝基苯胺 在 immobilized thermolysin 作用下， 以 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 反应 1.0h， 以90%的产率得到Z-丙氨酸-丙氨酸-丙氨酸-pNA
  参考文献：
  名称：

  有机介质中肽合成中的修饰蛋白酶

  摘要：

  我们表明，修饰的蛋白酶可以在有机溶剂中的溶液和固相上催化各种长度和结构各异的肽的合成。研究了以下修饰的蛋白酶，作为在极性有机溶剂（乙腈，二甲基甲酰胺和乙醇）中酶促肽合成的催化剂：吸附在硅藻土上的胃蛋白酶，枯草杆菌蛋白酶与十二烷基硫酸钠的非共价复合物，以及枯草杆菌蛋白酶或嗜热菌蛋白酶共价固定在聚乙烯基冷冻凝胶上醇。枯草杆菌蛋白酶与十二烷基硫酸钠和固定的枯草杆菌蛋白酶的非共价复合物的使用对于多肽片段的片段缩合特别有希望，该片段包含侧链中带有未保护离子源基团的三官能氨基酸残基，例如Lys，Arg，His，Glu和Asp 。

  DOI：

  10.1023/a:1026061828077

文献信息

• Peptide Synthesis in Organic Media with the Use of Subtilisin 72 Immobilized on a Poly(Vinyl Alcohol) Cryogel
  作者：A. V. Belyaeva、A. V. Bacheva、E. S. Oksenoit、E. N. Lysogorskaya、V. I. Lozinskii、I. Yu. Filippova

  DOI：10.1007/s11171-005-0072-y

  日期：2005.11

  Subtilisin 72 serine protease (EC 3.4.21.14) immobilized on a poly(vinyl alcohol) cryogel was used as a catalyst in the syntheses of N-protected peptide p-nitroanilides of the general formulas Z(or Boc)-Xaa-Phe-pNA (Xaa = Leu or Ala), Z-Ala-Xaa-Yaa-pNA (Xaa = Leu or Ala; Yaa = Leu or Phe), and Z-Ala-Ala-Xaa-Yaa-pNA (Xaa = Leu, Arg, or Gly; Yaa = Phe, Leu, Gly, Asp, or Glu). The syntheses were carried out in DMF-acetonitrile mixtures. A number of protected di-, tri-, and tetrapeptides were prepared in yields up to 99%. The syntheses were found to retain stereoselectivity under the conditions studied. The activation of carboxyl group of the acylating component was shown to have a positive effect upon the coupling rate.

  将固定于聚乙烯醇冻胶上的72丝氨酸蛋白酶（EC 3.4.21.14）用作合成N-保护肽对硝基苯胺的催化剂，其通式为Z（或Boc）-Xaa-Phe-pNA（Xaa=亮氨酸或丙氨酸）、Z-Ala-Xaa-Yaa-pNA（Xaa=亮氨酸或丙氨酸；Yaa=亮氨酸或苯丙氨酸）和Z-Ala-Ala-Xaa-Yaa-pNA（Xaa=亮氨酸、精氨酸或甘氨酸；Yaa=苯丙氨酸、亮氨酸、甘氨酸、天冬氨酸或谷氨酸）。合成在DMF-乙腈混合物中进行。制备了一系列二肽、三肽和四肽保护物，收率高达99%。研究发现，在所研究的条件下，合成保留了立体选择性。酰化成分羧基的活化对偶联率有积极影响。
• Isolation and Some Properties of a Serine Protease from the Fruits of<i>Cudrania cochinchinensis</i>(Lour.) Kudo et Masam.
  作者：Tetsuya UCHIKOBA、Kazunari ARIMA、Masayuki SHIMADA、Hiroo YONEZAWA、Mokoto KANEDA

  DOI：10.1271/bbb.64.623

  日期：2000.1

  An endopeptidase (Cudrania protease) with a molecular mass of 76 kDa has been purified from the fruits of Cudrania cochinchinensis (Lour.) Kudo et Masam. The enzyme was stable between pH 6 and 10 at 30°C for 60 min. The enzyme activity was inhibited by diisopropyl fluorophosphate, chymostatin, and aprotinin, but not by EDTA or pepstatin. These results indicated that the enzyme was a serine protease.

  从 Cudrania cochinchinensis (Lour.) Kudo et Masam 的果实中纯化出了一种分子质量为 76 kDa 的内肽酶（Cudrania 蛋白酶）。在 30°C 条件下，该酶在 pH 值 6 和 10 之间稳定 60 分钟。该酶的活性受氟磷酸二异丙酯、糜蛋白酶和阿普罗汀的抑制，但不受乙二胺四乙酸乙二酯（EDTA）和胃蛋白酶的抑制。这些结果表明该酶是一种丝氨酸蛋白酶。
• Biocatalytic properties of thermolysin immobilized on polyvinyl alcohol cryogel
  作者：A. V. Belyaeva、Yu. A. Smirnova、E. N. Lysogorskaya、E. S. Oksenoit、A. V. Timofeeva、V. I. Lozinskii、I. Yu. Filippova

  DOI：10.1134/s1068162008040079

  日期：2008.7

  Preparations with different contents of thermolysin were obtained by the immobilization of the enzyme on granulated polyvinyl alcohol cryogel. Their activity and stability in an aqueous medium and in mixtures of polar organic solvents of different composition were investigated. The catalytic properties of the preparations in reactions of peptide bond formation were studied, and the optimal amount of the biocatalyst, the concentrations of initial reagents, and the ratios of organic solvents and water necessary for effective enzymatic peptide synthesis catalyzed by immobilized thermolysin were determined. A series of peptides of the general formula Z-Ala-Ala-Xaa-pNA, where Xaa = Leu, Ile, Phe, Val, or Ala, were synthesized, and the immobilized enzyme was shown to retain substrate specificity in an organic medium.
• SDS-Subtilisin complex efficiently catalyzes synthesis of peptides in ethanol and 2-propanol
  作者：Irina V. Getun、Irina Yu. Filippova、Elena N. Lysogorskaya、Elena S. Oksenoit、Veronika V. Anisimova、Svetlana V. Kolobanova、Anna V. Bacheva、Valentin M. Stepanov

  DOI：10.1016/s0960-894x(97)10058-0

  日期：1997.10

  An enzymatic synthesis of tripeptide Z-Ala-Ala-Leu-pNA, tetrapeptides Z-Ala-Ala-P-1-P-1'-Xaa, where P-1 = Leu, Trp, Met, Ala, Ile, Phe; P-1' = Phe, Ala, Leu; Xaa = pNA, NH2, pentapeptides Z-Ala-Ala-Leu-Ala-Ala-pNA and Z-Ala-Ala-Leu-Ala-Phe-pNA is described. The reactions were performed in organic solvents using SDS-subtilisin complex as a catalyst of the peptide bond synthesis. (C) 1997 Elsevier Science Ltd.
• ——
  作者：I. Yu. Filippova、A. V. Bacheva、O. V. Baibak、F. M. Plieva、E. N. Lysogorskaya、E. S. Oksenoit、V. I. Lozinsky

  DOI：10.1023/a:1014350600760

  日期：——

  Covalent immobilization of subtilisin and thermolysin on cryogel of poly(vinyl alcohol) was carried out. The biocatalysts obtained are characterized by high stability in water and in DMF-MeCN mixtures of various compositions. The synthetic efficiency of immobilized subtilisin in the multiple iterative synthesis of the peptide Z-Ala-Ala-Leu-Phe-pNA was examined in organic mixtures of different solvent compositions, Immobilized subtilisin exhibits high synthetic activity in organic media. A series of N-acylated p-nitroanilides of tetrapeptides of the general formula Z-Ala-Ala-Xaa-Yaa-pNA (Z is benzyloxycarbonyl, Xaa = Leu, Lys, or Glu, Yaa = Phe or Asp; pNA = 4-NO2-C6H4NH-) were synthesized in 70-98% yields using immobilized subtilisin as a biocatalyst without activation and protection of the ionogenic groups of polyfunctional amino acids. Immobilized thermolysin in a DMF-MeCN mixture catalyzed the formation of the peptide Z-Ala-Ala-Leu-pNA, which was obtained in 90% yield (during 1 h). It was demonstrated that the biocatalyst can be used repeatedly and that it retained activity after storage in an aqueous buffer during 6 months.