Ac-Tyr-Ala-Ala-Tyr-Ala-Gly-OH

• 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: Ac-Tyr-Ala-Ala-Tyr-Ala-Gly-OH
• 英文别名: 2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]propanoyl]amino]propanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]propanoyl]amino]acetic acid
• 化学式: C₃₁H₄₀N₆O₁₀
• 分子量: 656.693
• InChiKey: ZSRIIWHTPJRWME-NRYBCHEISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.6
• 重原子数：
  47
• 可旋转键数：
  16
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.39
• 拓扑面积：
  252
• 氢给体数：
  9
• 氢受体数：
  10

反应信息

• 作为产物：
  描述：

  N-乙酰-L-酪氨酸乙酯 、 H-Ala-Ala-Tyr-Ala-Gly-OH 在 sodium chloride 、 calcium chloride 、 α-chymotrypsin 作用下， 以61.2%的产率得到Ac-Tyr-Ala-Ala-Tyr-Ala-Gly-OH
  参考文献：
  名称：

  Effect of freezing on the enzymatic coupling of specific amino acid-containing peptide fragments

  摘要：

  The effect of freezing on the enzymatic coupling of highly specific amino acid-containing peptide fragments was investigated using trypsin, a-chymotrypsin, and Bacillus licheniformis Glu-specific endopeptidase as biocatalysts. Comparison with reactions at normal temperature indicates that freezing efficiently represses the cleavage of specific peptide bonds independent of their individual localisation and specificity achieving irreversible and efficient peptide bond formation without proteolytic side reactions. (C) 2000 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0957-4166(00)00187-7

文献信息

• Effect of freezing on the enzymatic coupling of specific amino acid-containing peptide fragments
  作者：Nicole Wehofsky、Marion Haensler、Sebastian W Kirbach、Johannes-Dieter Wissmann、Frank Bordusa

  DOI：10.1016/s0957-4166(00)00187-7

  日期：2000.6

  The effect of freezing on the enzymatic coupling of highly specific amino acid-containing peptide fragments was investigated using trypsin, a-chymotrypsin, and Bacillus licheniformis Glu-specific endopeptidase as biocatalysts. Comparison with reactions at normal temperature indicates that freezing efficiently represses the cleavage of specific peptide bonds independent of their individual localisation and specificity achieving irreversible and efficient peptide bond formation without proteolytic side reactions. (C) 2000 Elsevier Science Ltd. All rights reserved.