(S)-2-(methylamino)-3-(7-(3-methylbut-2-en-1-yl)-1H-indol-3-yl)propanoic acid | 1049019-50-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吲哚及其衍生物
• 英文名称: (S)-2-(methylamino)-3-(7-(3-methylbut-2-en-1-yl)-1H-indol-3-yl)propanoic acid
• CAS: 1049019-50-2
• 化学式: C₁₇H₂₂N₂O₂
• 分子量: 286.374
• InChiKey: DGQBQFDENAQAQN-HNNXBMFYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.89
• 重原子数：
  21.0
• 可旋转键数：
  6.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  65.12
• 氢给体数：
  3.0
• 氢受体数：
  2.0

反应信息

• 作为产物：
  描述：

  3-甲基丁-2-烯基膦酰磷酸氢酯 、 相思豆毒素 在 7-dimethylallyl tryptophan synthase from fungusNeosartorya sp. in E_. coli 、 calcium chloride 作用下， 以 aq. buffer 为溶剂， 反应 16.0h， 生成 (S)-2-(methylamino)-3-(7-(3-methylbut-2-en-1-yl)-1H-indol-3-yl)propanoic acid
  参考文献：
  名称：

  A 7-dimethylallyl tryptophan synthase from a fungal Neosartorya sp.: Biochemical characterization and structural insight into the regioselective prenylation

  摘要：

  A putative 7-dimethylallyl tryptophan synthase (DMATS) gene from a fungal Neosartorya sp. was cloned and overexpressed as a soluble His(6)-fusion protein in Escherichia coli. The enzyme was found to catalyze the prenylation of L-tryptophan at the C7 position of the indole moiety in the presence of dimethylallyl diphosphate; thus, it functions as a 7-DMATS. In this study, we describe the biochemical characterization of 7-DMATS from Neosartorya sp., referred to as 7-DMATS(Neo), and the structural basis of the regioselective prenylation of L-tryptophan at the C7 position by comparison of the three-dimensional structural models of 7-DMATS(Neo) with FgaPT2 (4-DMATS) from Aspergillus fumigatus. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2014.02.031

文献信息

• A 7-dimethylallyl tryptophan synthase from a fungal Neosartorya sp.: Biochemical characterization and structural insight into the regioselective prenylation
  作者：Kengo Miyamoto、Fumihiro Ishikawa、Shinya Nakamura、Yutaka Hayashi、Isao Nakanishi、Hideaki Kakeya

  DOI：10.1016/j.bmc.2014.02.031

  日期：2014.4

  A putative 7-dimethylallyl tryptophan synthase (DMATS) gene from a fungal Neosartorya sp. was cloned and overexpressed as a soluble His(6)-fusion protein in Escherichia coli. The enzyme was found to catalyze the prenylation of L-tryptophan at the C7 position of the indole moiety in the presence of dimethylallyl diphosphate; thus, it functions as a 7-DMATS. In this study, we describe the biochemical characterization of 7-DMATS from Neosartorya sp., referred to as 7-DMATS(Neo), and the structural basis of the regioselective prenylation of L-tryptophan at the C7 position by comparison of the three-dimensional structural models of 7-DMATS(Neo) with FgaPT2 (4-DMATS) from Aspergillus fumigatus. (C) 2014 Elsevier Ltd. All rights reserved.