BocTyrLeuNH2 | 126028-17-9

• 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: BocTyrLeuNH2
• 英文别名: Boc-Tyr-Leu-NH2；tert-butyl N-[(2S)-1-[[(2S)-1-amino-4-methyl-1-oxopentan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]carbamate
• CAS: 126028-17-9
• 化学式: C₂₀H₃₁N₃O₅
• 分子量: 393.483
• InChiKey: CSLUYTYTLGOUEE-HOTGVXAUSA-N

物化性质

• 沸点：
  668.4±55.0 °C(Predicted)
• 密度：
  1.160±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  28
• 可旋转键数：
  10
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.55
• 拓扑面积：
  131
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  亮氨酰胺 、 Boc-L-酪氨酸甲酯 在 subtilisin-CLEC 作用下， 以 乙腈 为溶剂， 反应 120.0h， 以90%的产率得到BocTyrLeuNH2
  参考文献：
  名称：

  Cross-Linked Crystals of Subtilisin:  Versatile Catalyst for Organic Synthesis

  摘要：

  Cross-linked enzyme crystals (CLECs) of subtilisin exhibit excellent activity in aqueous and various organic solvents. This catalyst is more stable than the native enzyme in both aqueous and mixed aqueous/organic solutions. Subtilisin-CLEC was shown to be a versatile catalyst. It was used for the syntheses of peptides and peptidomimetics, mild hydrolysis of amino acid and peptide amides, enantio- and regioselective reactions, and transesterifications.

  DOI：

  10.1021/jo9618334

文献信息

• Enzymatic peptide syntheses in organic solvent mediated by modified α-chymotrypsin
  作者：Marie-Thérèse Babonneau、Robert Jacquier、René Lazaro、Philippe Viallefont

  DOI：10.1016/s0040-4039(00)99125-1

  日期：1989.1

  Peptide couplings have been catalyzed in organic medium containing a slight amount of water (<0,5%) by PEG modified α-Chymotrypsin.

  肽偶联已通过PEG修饰的α-胰凝乳蛋白酶在含有少量水（<0.5％）的有机介质中催化。
• Immobilized<i>Aspergillus Oryzae</i>Protease Catalyzed Formation of Peptide Bonds in Organic Solvent
  作者：Ing-Lung Shih、Yun-Yin Lin、Hui-Yao Huang、Dar-Fu Tai、Kuan-Chu Chen

  DOI：10.1002/jccs.199700049

  日期：1997.6

  AbstractImmobilized Aspergillus oryzae protease (AOP) catalyzed the formation of peptide bonds between TV‐protected amino acids and amino acid esters or amides in ethyl acetate. The influences of pH and reaction time on the coupling of Boc‐L‐Tyr and Gly‐NH2 were studied. The optimal reaction condition for this enzyme catalyzed synthesis of Boc‐L‐Phe‐Gly‐NH2 (98.66%) was at pH 5.5 and a duration of 48 hours.
• Methyltrypsin-Catalyzed Peptide Coupling: Comparison of Alkyl Ester and Guanidinophenyl Ester Derivatives as Acyl Donor Component
  作者：Kunihiko Itoh、Haruo Sekizaki、Eiko Toyota、Kazutaka Tanizawa

  DOI：10.1006/bioo.1997.1076

  日期：1997.10

  Methyltrypsin-catalyzed peptide synthesis has been studied by using conventional alkyl ester and p-guanidinophenyl ester derivatives of alpha-amino acid as the acyl donor component. They were found to be coupled with alpha-amino acid derivatives (acyl acceptor component) to produce dipeptide. The behavior of methyltrypsin toward both the substrates has been studied. (C) 1997 Academic Press.
• New biocatalysts for peptide synthesis :Gels of copolymerized acrylic derivatives of α-chymotrypsin and polyoxyethylene
  作者：Valérie Fulcrand、Robert Jacquier、René Lazaro、Philippe Viallefont

  DOI：10.1016/s0040-4020(01)90526-5

  日期：1990.1
• BABONNEAU, MARIE-THERESE;JACQUIER, ROBERT;LAZARO, RENE;VIALLEFONT, PHILIP+, TETRAHEDRON LETT., 30,(1989) N1, C. 2787-2790
  作者：BABONNEAU, MARIE-THERESE、JACQUIER, ROBERT、LAZARO, RENE、VIALLEFONT, PHILIP+

  DOI：——

  日期：——