methyl rac-[11-13C]-4-(1-hydroxyethyl)quinolne-2-carboxylate | 179764-61-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 喹啉及其衍生物
• 英文名称: methyl rac-[11-13C]-4-(1-hydroxyethyl)quinolne-2-carboxylate
• 英文别名: methyl rac-[11-¹³C]-4-(1-hydroxyethyl)quinolne-2-carboxylate
• CAS: 179764-61-5
• 化学式: C₁₃H₁₃NO₃
• 分子量: 232.24
• InChiKey: VFCIMUKXFDKTTA-KCKQSJSWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.07
• 重原子数：
  17.0
• 可旋转键数：
  2.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.23
• 拓扑面积：
  59.42
• 氢给体数：
  1.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  methyl rac-[11-13C]-4-(1-hydroxyethyl)quinolne-2-carboxylate 在 sodium hydroxide 作用下， 以 四氢呋喃 为溶剂， 反应 2.0h， 生成 rac-[11-¹³C]-4-(1-hydroxyethyl)quinolne-2-carboxylic acid
  参考文献：
  名称：

  Studies on the biosynthesis of thiostrepton: 4-(1-hydroxyethyl)quinoline-2-carboxylate as a free intermediate on the pathway to the quinaldic acid moiety

  摘要：

  Specifically C-13-labeled quinoline-2-carboxylate derivatives were synthesized from quinoline and used to study the biosynthesis of thiostrepton in a strain of Streptomyces laurentii. C-13 NMR analysis of thiostrepton recovered after feeding methyl (RS)-[11-C-13]-4-(1-hydroxyethyl)quinoline-2-carboxylate or methyl [11-C-13]-4-acetylquinoline-2-carboxylate showed conclusively that these compounds are specifically and efficiently incorporated into thiostrepton. Both compounds were also detected in cultures of the producing organism by isotope dilution analysis. The significance of the relative endogenous concentrations of the two compounds and of the relative extent of the incorporation of exogenously added labeled material into thiostrepton are discussed in terms of the biosynthetic pathway linking tryptophan and 4-(1-hydroxyethyl)quinoline-2-carboxylate in S. laurentii. A highly specific enzyme activity was detected in cell-free extracts of S. laurentii that was capable of adenylating (12S)-4-(1-hydroxyethyl)quinoline-2-carboxylic acid. Partial purification of the enzyme was achieved. The enzyme was found to be specific for the enantiomer of the substrate which has the same absolute configuration as found in the natural antibiotic structure. The presence of one specific enzyme catalysing the adenylation process in S. laurentii was shown by photoaffinity labeling with [alpha-P-32]-8-azido-ATP and subsequent SDS PAGE analysis of the labeled products. The native molecular weight of the active enzyme, determined by gel permeation chromatography, was found to be approximately 47 kDa, compared with a denatured weight of 50 kDa estimated for the photoaffinity-labeled protein. The enzyme is thus probably monomeric. Copyright (C) 1996 Elsevier Science Ltd

  DOI：

  10.1016/0968-0896(96)00126-5
• 作为产物：
  描述：

  [11-13C]-N-benzoyl-2-cyano-1,2-dihydroquinoline 在 sodium hydroxide 、 sodium tetrahydroborate 、 氯化亚砜 、 氢溴酸 、 双氧水 、 iron(II) sulfate 、 溶剂黄146 、 三氟乙酸 作用下， 以 甲醇 为溶剂， 反应 25.91h， 生成 methyl rac-[11-13C]-4-(1-hydroxyethyl)quinolne-2-carboxylate
  参考文献：
  名称：

  Studies on the biosynthesis of thiostrepton: 4-(1-hydroxyethyl)quinoline-2-carboxylate as a free intermediate on the pathway to the quinaldic acid moiety

  摘要：

  Specifically C-13-labeled quinoline-2-carboxylate derivatives were synthesized from quinoline and used to study the biosynthesis of thiostrepton in a strain of Streptomyces laurentii. C-13 NMR analysis of thiostrepton recovered after feeding methyl (RS)-[11-C-13]-4-(1-hydroxyethyl)quinoline-2-carboxylate or methyl [11-C-13]-4-acetylquinoline-2-carboxylate showed conclusively that these compounds are specifically and efficiently incorporated into thiostrepton. Both compounds were also detected in cultures of the producing organism by isotope dilution analysis. The significance of the relative endogenous concentrations of the two compounds and of the relative extent of the incorporation of exogenously added labeled material into thiostrepton are discussed in terms of the biosynthetic pathway linking tryptophan and 4-(1-hydroxyethyl)quinoline-2-carboxylate in S. laurentii. A highly specific enzyme activity was detected in cell-free extracts of S. laurentii that was capable of adenylating (12S)-4-(1-hydroxyethyl)quinoline-2-carboxylic acid. Partial purification of the enzyme was achieved. The enzyme was found to be specific for the enantiomer of the substrate which has the same absolute configuration as found in the natural antibiotic structure. The presence of one specific enzyme catalysing the adenylation process in S. laurentii was shown by photoaffinity labeling with [alpha-P-32]-8-azido-ATP and subsequent SDS PAGE analysis of the labeled products. The native molecular weight of the active enzyme, determined by gel permeation chromatography, was found to be approximately 47 kDa, compared with a denatured weight of 50 kDa estimated for the photoaffinity-labeled protein. The enzyme is thus probably monomeric. Copyright (C) 1996 Elsevier Science Ltd

  DOI：

  10.1016/0968-0896(96)00126-5