5-(1,4-dimethylpentylamino)-3-methyl-1,2-benzoquinone | 1350887-83-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 5-(1,4-dimethylpentylamino)-3-methyl-1,2-benzoquinone
• 英文别名: 3-Methyl-5-(5-methylhexan-2-ylamino)cyclohexa-3,5-diene-1,2-dione；3-methyl-5-(5-methylhexan-2-ylamino)cyclohexa-3,5-diene-1,2-dione
• CAS: 1350887-83-0
• 化学式: C₁₄H₂₁NO₂
• 分子量: 235.326
• InChiKey: IZAMJXFCAHNPKV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  17
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.57
• 拓扑面积：
  46.2
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  2-氨基-5-甲基己烷 、 3-甲基苯邻二酚 在 Pycnoporus cinnabarinus SBUG-M 1044 laccase 作用下， 以 甲醇 为溶剂， 反应 2.0h， 以81%的产率得到5-(1,4-dimethylpentylamino)-3-methyl-1,2-benzoquinone
  参考文献：
  名称：

  C–N coupling of 3-methylcatechol with primary amines using native and recombinant laccases from Trametes versicolor and Pycnoporus cinnabarinus

  摘要：

  Five laccase genes from Pycnoporus cinnabarinus and Trametes versicolor encoding for different isoenzymes have been cloned, recombinantly expressed and characterized. Following C-N coupling of primary linear, branched-chained and cyclic amines to 3-methylcatechol was mediated by native and recombinant laccases yielding the corresponding secondary amines. Formation of C5-monoaminated ortho-methylquinones occurred within 1-2 h; prolonged incubation led to the formation of high-molecular mass products. No difference between the use of native or recombinant isoenzymes from P. cinnabannus or T versicolor was observed. Optimization of the reaction conditions included variation of amine donor ratios, pH, amount and type of enzyme preparations. The formation of by-products could be suppressed at pH values corresponding to the enzymes optima (pH 4-5). A total of 10 secondary amines were synthesized with product formations of up to 80%. Furthermore, all purified secondary amines were characterized by NMR-, LC-MS- and HRMS-analysis and log P values were determined. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2011.09.123

文献信息

• C–N coupling of 3-methylcatechol with primary amines using native and recombinant laccases from Trametes versicolor and Pycnoporus cinnabarinus
  作者：Susanne Herter、Annett Mikolasch、Dirk Michalik、Elke Hammer、Frieder Schauer、Uwe Bornscheuer、Marlen Schmidt

  DOI：10.1016/j.tet.2011.09.123

  日期：2011.12

  Five laccase genes from Pycnoporus cinnabarinus and Trametes versicolor encoding for different isoenzymes have been cloned, recombinantly expressed and characterized. Following C-N coupling of primary linear, branched-chained and cyclic amines to 3-methylcatechol was mediated by native and recombinant laccases yielding the corresponding secondary amines. Formation of C5-monoaminated ortho-methylquinones occurred within 1-2 h; prolonged incubation led to the formation of high-molecular mass products. No difference between the use of native or recombinant isoenzymes from P. cinnabannus or T versicolor was observed. Optimization of the reaction conditions included variation of amine donor ratios, pH, amount and type of enzyme preparations. The formation of by-products could be suppressed at pH values corresponding to the enzymes optima (pH 4-5). A total of 10 secondary amines were synthesized with product formations of up to 80%. Furthermore, all purified secondary amines were characterized by NMR-, LC-MS- and HRMS-analysis and log P values were determined. (C) 2011 Elsevier Ltd. All rights reserved.