trans-cinnamic acid-β,2,3,4,5,6-d6 | 1174218-97-3

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 肉桂酸及其衍生物
• 英文名称: trans-cinnamic acid-β,2,3,4,5,6-d6
• 英文别名: 3-Phenyl-d5-2-propenoic acid-3-d1；(E)-3-deuterio-3-(2,3,4,5,6-pentadeuteriophenyl)prop-2-enoic acid
• CAS: 1174218-97-3
• 化学式: C₉H₈O₂
• 分子量: 154.114
• InChiKey: WBYWAXJHAXSJNI-UMENIHJVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.1
• 重原子数：
  11
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  37.3
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  trans-cinnamic acid-β,2,3,4,5,6-d6 、 三甲基硅烷化重氮甲烷 以 甲醇 、 乙酸乙酯 为溶剂， 生成
  参考文献：
  名称：

  Stereochemistry and Mechanism of a Microbial Phenylalanine Aminomutase

  摘要：

  The stereochemistry of a phenylalanine aminomutase (PAM) on the andrimid biosynthetic pathway in Pantoea agglomerans (Pa) is reported. PaPAM is a member of the 4-methylidene-1H-imidazol-5(4H)-one (MIO)-dependent family of catalysts and isomerizes (2S)-alpha-phenylalanine to (3S)-beta-phenylalanine, which is the enantiomer of the product made by the mechanistically similar aminomutase TcPAM from Taxus plants. The NH2 and pro-(3S) hydrogen groups at C-alpha and C-beta, respectively, of the substrate are removed and interchanged completely intramolecularly with inversion of configuration at the migration centers to form P-phenylalanine. This is a contrast to the retention of configuration mechanism followed by TcPAM.

  DOI：

  10.1021/ja2030728
• 作为产物：
  描述：

  [ring, 3-(2)H6]-(2RS,3SR)-α-phenylalanine 在 Rhodotorula glutinis phenylalanine ammonia lyase 作用下， 反应 1.0h， 生成 trans-cinnamic acid-β,2,3,4,5,6-d6
  参考文献：
  名称：

  Stereochemistry and Mechanism of a Microbial Phenylalanine Aminomutase

  摘要：

  The stereochemistry of a phenylalanine aminomutase (PAM) on the andrimid biosynthetic pathway in Pantoea agglomerans (Pa) is reported. PaPAM is a member of the 4-methylidene-1H-imidazol-5(4H)-one (MIO)-dependent family of catalysts and isomerizes (2S)-alpha-phenylalanine to (3S)-beta-phenylalanine, which is the enantiomer of the product made by the mechanistically similar aminomutase TcPAM from Taxus plants. The NH2 and pro-(3S) hydrogen groups at C-alpha and C-beta, respectively, of the substrate are removed and interchanged completely intramolecularly with inversion of configuration at the migration centers to form P-phenylalanine. This is a contrast to the retention of configuration mechanism followed by TcPAM.

  DOI：

  10.1021/ja2030728
• 作为试剂：
  描述：

  L-苯丙氨酸-15N 在 Pantoea agglomerans phenylalanine aminomutase 、 trans-cinnamic acid-β,2,3,4,5,6-d6 、 苯甲酰乙酸乙酯 、 sodium hydroxide 作用下， 生成
  参考文献：
  名称：

  Stereochemistry and Mechanism of a Microbial Phenylalanine Aminomutase

  摘要：

  The stereochemistry of a phenylalanine aminomutase (PAM) on the andrimid biosynthetic pathway in Pantoea agglomerans (Pa) is reported. PaPAM is a member of the 4-methylidene-1H-imidazol-5(4H)-one (MIO)-dependent family of catalysts and isomerizes (2S)-alpha-phenylalanine to (3S)-beta-phenylalanine, which is the enantiomer of the product made by the mechanistically similar aminomutase TcPAM from Taxus plants. The NH2 and pro-(3S) hydrogen groups at C-alpha and C-beta, respectively, of the substrate are removed and interchanged completely intramolecularly with inversion of configuration at the migration centers to form P-phenylalanine. This is a contrast to the retention of configuration mechanism followed by TcPAM.

  DOI：

  10.1021/ja2030728

文献信息

• Alternative Pathway to the Formation of <i>trans</i>-Cinnamic Acid Derived from <scp>l</scp>-Phenylalanine in Tea (<i>Camellia sinensis</i>) Plants and Other Plants
  作者：Lanting Zeng、Xiaoqin Wang、Haibo Tan、Yinyin Liao、Ping Xu、Ming Kang、Fang Dong、Ziyin Yang

  DOI：10.1021/acs.jafc.9b07467

  日期：2020.3.18

  trans-Cinnamic acid (CA) is a precursor of many phenylpropanoid compounds, including catechins and aroma compounds, in tea (Camellia sinensis) leaves and is derived from L-phenylalanine (L-Phe) deamination. We have discovered an alternative CA formation pathway from L-Phe via phenylpyruvic acid (PPA) and phenyllactic acid (PAA) in tea leaves through stable isotope-labeled precursor tracing and enzyme reaction evidence. Both PPA reductase genes (CsPPARs) involved in the PPA-to-PAA pathway were isolated from tea leaves and functionally characterized in vitro and in vivo. CsPPAR1 and CsPPAR2 transformed PPA into PAA and were both localized in the leaf cell cytoplasm. Rosa hybrida flowers (economic crop flower), Lycopersicon esculentum Mill. fruits (economic crop fruit), and Arabidopsis thaliana leaves (leaf model plant) also contained this alternative CA formation pathway, suggesting that it occurred in most plants, regardless of different tissues and species. These results improve our understanding of CA biosynthesis in tea plants and other plants.
• Stereochemistry and Mechanism of a Microbial Phenylalanine Aminomutase
  作者：Nishanka Dilini Ratnayake、Udayanga Wanninayake、James H. Geiger、Kevin D. Walker

  DOI：10.1021/ja2030728

  日期：2011.6.8

  The stereochemistry of a phenylalanine aminomutase (PAM) on the andrimid biosynthetic pathway in Pantoea agglomerans (Pa) is reported. PaPAM is a member of the 4-methylidene-1H-imidazol-5(4H)-one (MIO)-dependent family of catalysts and isomerizes (2S)-alpha-phenylalanine to (3S)-beta-phenylalanine, which is the enantiomer of the product made by the mechanistically similar aminomutase TcPAM from Taxus plants. The NH2 and pro-(3S) hydrogen groups at C-alpha and C-beta, respectively, of the substrate are removed and interchanged completely intramolecularly with inversion of configuration at the migration centers to form P-phenylalanine. This is a contrast to the retention of configuration mechanism followed by TcPAM.