(S)-2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-(4-hydroxy-2-methyl-phenyl)-propionic acid | 1145678-75-6

• 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: (S)-2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-(4-hydroxy-2-methyl-phenyl)-propionic acid
• 英文别名: N-[(9H-Fluoren-9-ylmethoxy)carbonyl]-2-methyl-L-tyrosine；(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-(4-hydroxy-2-methylphenyl)propanoic acid
• CAS: 1145678-75-6
• 化学式: C₂₅H₂₃NO₅
• 分子量: 417.461
• InChiKey: MEFNXNKFGAIWBC-QHCPKHFHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.7
• 重原子数：
  31
• 可旋转键数：
  7
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.2
• 拓扑面积：
  95.9
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  间甲酚 在 tyrosine phenol-lyase 、 氨 、 sodium carbonate 作用下， 以 1,4-二氧六环 为溶剂， 生成 (S)-2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-(4-hydroxy-2-methyl-phenyl)-propionic acid
  参考文献：
  名称：

  Tyrosine analogues as alternative substrates for protein tyrosine kinase Csk: Insights into substrate selectivity and catalytic mechanism

  摘要：

  Protein tyrosine kinases are critical enzymes in cell signal transduction but relatively little is known about the molecular recognition of the tyrosine substrate by these enzymes. Details of tyrosine substrate specificity within the context of a short peptide were investigated for protein tyrosine kinase Csk. It was found that aryl ring functional group substitutions the size of methyl group or smaller were generally well tolerated by the protein tyrosine kinase Csk whereas larger groups caused a decline in substrate efficiency. Extension of the phenol from the peptide backbone by a single methylene was acceptable for phosphorylation whereas removal of a methylene nearly abolished reactivity. Only the L-tyrosine derivative was processed. A negative charge ortho to the phenol hydroxyl was incompatible with substrate reactivity, consistent with previous pH rate profiles which indicated the importance of the neutral phenol. Overall, these studies confirmed the interpretation of a previous linear free energy relationship analysis which suggested that the enzyme followed a dissociative transition state mechanism. (C) 2000 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(00)00053-5

文献信息

• Tyrosine analogues as alternative substrates for protein tyrosine kinase Csk: Insights into substrate selectivity and catalytic mechanism
  作者：Kyonghee Kim、Keykavous Parang、Ontario D Lau、Philip A Cole

  DOI：10.1016/s0968-0896(00)00053-5

  日期：2000.6

  Protein tyrosine kinases are critical enzymes in cell signal transduction but relatively little is known about the molecular recognition of the tyrosine substrate by these enzymes. Details of tyrosine substrate specificity within the context of a short peptide were investigated for protein tyrosine kinase Csk. It was found that aryl ring functional group substitutions the size of methyl group or smaller were generally well tolerated by the protein tyrosine kinase Csk whereas larger groups caused a decline in substrate efficiency. Extension of the phenol from the peptide backbone by a single methylene was acceptable for phosphorylation whereas removal of a methylene nearly abolished reactivity. Only the L-tyrosine derivative was processed. A negative charge ortho to the phenol hydroxyl was incompatible with substrate reactivity, consistent with previous pH rate profiles which indicated the importance of the neutral phenol. Overall, these studies confirmed the interpretation of a previous linear free energy relationship analysis which suggested that the enzyme followed a dissociative transition state mechanism. (C) 2000 Elsevier Science Ltd. All rights reserved.