1,1-diethoxybut-3-en-2-ol | 143106-73-4

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 1,1-diethoxybut-3-en-2-ol
• 英文别名: 4,4-diethoxybut-1-en-3-ol
• CAS: 143106-73-4
• 化学式: C₈H₁₆O₃
• 分子量: 160.213
• InChiKey: DSZHIRKLQRADHJ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  11
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  38.7
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  1,1-diethoxybut-3-en-2-ol 在 盐酸 作用下， 反应 30.0h， 生成 (+/-)-2-hydroxy-3-butenal
  参考文献：
  名称：

  Transketolase from Escherichia coli: A practical procedure for using the biocatalyst for asymmetric carbon-carbon bond synthesis

  摘要：

  A practical procedure is reported for the use of the enzyme transketolase, from Escherichia coli, for asymmetric carbon-carbon bond synthesis. The reactions with the biocatalyst are conveniently carried out, on a gram scale, in unbuffered aqueous media by employing a pH autotitrator. An improved large scale synthesis of hydroxypyruvate is also reported. Copyright (C) 1996 Elsevier Science Ltd

  DOI：

  10.1016/0957-4166(96)00266-2
• 作为产物：
  描述：

  丙烯醛缩二乙醇 在 2,3-二巯基丁二酸 、 臭氧 作用下， 以 四氢呋喃 为溶剂， 反应 88.0h， 生成 1,1-diethoxybut-3-en-2-ol
  参考文献：
  名称：

  Substrate specificity and carbohydrate synthesis using transketolase

  摘要：

  This paper describes the use of the enzyme transketolase as a catalyst in organic synthesis. The properties of transketolase from both yeast and spinach were investigated. The yeast enzyme was found to be more convenient for routine use. Examination of the substrate specificity of yeast transketolase demonstrated that the enzyme accepts a wide variety of 2-hydroxy aldehydes as substrates. A practical protocol for transketolase-catalyzed condensation of hydroxypyruvic acid with these aldehydes has been developed and used for the synthesis of four carbohydrates: L-idose, L-gulose, 2-deoxy-L-xylohexose, and L-xylose.

  DOI：

  10.1021/jo00048a023

文献信息

• Fructose-6-phosphate aldolases as versatile biocatalysts for nitrocyclitol syntheses
  作者：Flora Camps Bres、Christine Guérard-Hélaine、Carlos Fernandes、José A. Castillo、Marielle Lemaire

  DOI：10.1016/j.tetasy.2013.07.016

  日期：2013.9

  Efficient and stereoselective polyhydroxylated nitrocyclitol syntheses were performed via biocatalysed aldol reactions. The key step was based on a one-pot/one-enzyme cascade reaction process where two reactions occur: aldolase-catalysed aldolisation and spontaneous intramolecular nitroaldolisation. The synthetic methodology was investigated using fructose-6-phosphate aldolase A129S for the synthesis of known nitrocyclitols. Improvements were obtained which involved less steps and increased yields. Several new nitrocyclitols were also prepared using hydroxyacetone (HA) as the donor and FSA wt. From nitrocyclitol stereochemical analyses, the intramolecular nitro-Henry reaction stereoselectivity was dependent on the donor substrate used, HA or dihydroxyacetone (DHA). Whereas DHA provided two stereoisomers, four were obtained using HA. (C) 2013 Elsevier Ltd. All rights reserved.
• Parrain, Jean-Luc; Beaudet, Isabelle; Cintrat, Jean-Christophe, Bulletin de la Societe Chimique de France, 1994, vol. 131, # 3, p. 304 - 312
  作者：Parrain, Jean-Luc、Beaudet, Isabelle、Cintrat, Jean-Christophe、Duchene, Alain、Quintard, Jean-Paul

  DOI：——

  日期：——
• Substrate specificity and carbohydrate synthesis using transketolase
  作者：Yoshihiro Kobori、David C. Myles、George M. Whitesides

  DOI：10.1021/jo00048a023

  日期：1992.10

  This paper describes the use of the enzyme transketolase as a catalyst in organic synthesis. The properties of transketolase from both yeast and spinach were investigated. The yeast enzyme was found to be more convenient for routine use. Examination of the substrate specificity of yeast transketolase demonstrated that the enzyme accepts a wide variety of 2-hydroxy aldehydes as substrates. A practical protocol for transketolase-catalyzed condensation of hydroxypyruvic acid with these aldehydes has been developed and used for the synthesis of four carbohydrates: L-idose, L-gulose, 2-deoxy-L-xylohexose, and L-xylose.
• Transketolase from Escherichia coli: A practical procedure for using the biocatalyst for asymmetric carbon-carbon bond synthesis
  作者：K.Gall Morris、Mark E.B. Smith、Nicholas J. Turner、Malcolm D. Lilly、Robin K. Mitra、John M. Woodley

  DOI：10.1016/0957-4166(96)00266-2

  日期：1996.8

  A practical procedure is reported for the use of the enzyme transketolase, from Escherichia coli, for asymmetric carbon-carbon bond synthesis. The reactions with the biocatalyst are conveniently carried out, on a gram scale, in unbuffered aqueous media by employing a pH autotitrator. An improved large scale synthesis of hydroxypyruvate is also reported. Copyright (C) 1996 Elsevier Science Ltd