β-Hydroxybutyramide | 24311-45-3

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: β-Hydroxybutyramide
• 英文别名: 3-hydroxybutyramide；3-hydroxybutyric acid；3-Hydroxy-buttersaeure-amid；3-Hydroxybuttersaeueamid；3-hydroxy-butyric acid amide；DL-3-Hydroxybuttersaeureamid；beta-hydroxybutyramide；3-Hydroxybutanamide
• CAS: 24311-45-3
• 化学式: C₄H₉NO₂
• mdl: MFCD19159499
• 分子量: 103.121
• InChiKey: OOHIGOIEQKKEPK-UHFFFAOYSA-N

物化性质

• 熔点：
  99-100 °C
• 沸点：
  315.9±25.0 °C(Predicted)
• 密度：
  1.105±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -1.2
• 重原子数：
  7
• 可旋转键数：
  2
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  63.3
• 氢给体数：
  2
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  β-Hydroxybutyramide 在 氢氧化钾 、 碘苯二乙酸 作用下， 以 甲醇 为溶剂， 反应 1.0h， 以68%的产率得到5-甲基-1,3-恶唑烷-2-酮
  参考文献：
  名称：

  邻氨基苯甲酰胺、水杨酰胺和一些β-取代酰胺的高价碘氧化重排：2-苯并咪唑酮、2-苯并恶唑酮和相关化合物的新型便捷合成

  摘要：

  在甲醇氢氧化钾中用碘苯二乙酸酯氧化邻氨基苯甲酰胺、水杨酰胺和一些β-取代的酰胺，分别导致2-苯并咪唑酮、2-苯并恶唑酮和相关化合物的新且方便的合成。该反应可能通过最初的霍夫曼型重排发生，然后是中间体异氰酸酯的分子内环化。

  DOI：

  10.1055/s-2001-12346
• 作为产物：
  描述：

  β-丁内酯 在 氨 作用下， 生成 β-Hydroxybutyramide
  参考文献：
  名称：

  Johansson, Chemisches Zentralblatt, 1916, vol. 87, # II, p. 557

  摘要：

  DOI：

文献信息

• Synthesis of silyl iron hydride <i>via</i> Si–H activation and its dual catalytic application in the hydrosilylation of carbonyl compounds and dehydration of benzamides
  作者：Shishuai Ren、Shangqing Xie、Tingting Zheng、Yangyang Wang、Shilu Xu、Benjing Xue、Xiaoyan Li、Hongjian Sun、Olaf Fuhr、Dieter Fenske

  DOI：10.1039/c8dt00289d

  日期：——

  The hydrido silyl iron complex (o-Ph2PC6H4SiMe2)Fe(PMe3)3H (2) was obtained via the activation of the Si–H bond of the bidentate silyl ligand o-Ph2P(C6H4)SiMe2H (1) by Fe(PMe3)4. 2 showed good to excellent catalytic activity in both the reduction of aldehydes/ketones and the dehydration of benzamide. In addition, with complex 2 as a catalyst, α,β-unsaturated carbonyls could be selectively reduced to

  氢化硅烷基铁络合物（o -Ph 2 PC 6 H 4 SiMe 2）Fe（PMe 3）3 H（2）是通过激活双齿甲硅烷基配体o -Ph 2 P（C）的Si–H键而获得的Fe（PMe 3）4形成6 H 4）SiMe 2 H（1）。图2在醛/酮的还原和苯甲酰胺的脱水中均显示出良好至优异的催化活性。另外，带复数2作为催化剂，α，β-不饱和羰基可以选择性地还原为相应的α，β-不饱和醇。提出了2的形成机理和催化脱水过程，并进行了部分实验验证。
• Highly Efficient Synthesis of Ureas and Carbamates from Amides by Iodosylbenzene-Induced Hofmann Rearrangement
  作者：Peng Liu、Zhiming Wang、Xianming Hu

  DOI：10.1002/ejoc.201101784

  日期：2012.4

  A simple and efficient method for the synthesis of 1,3-disubstituted ureas and carbamates from amides by using iodosylbenzene as the oxidant is described. Symmetric and asymmetric ureas and carbamates can be prepared by this procedure in up to 98 % yield. Ureidopeptides can also be prepared in good yield by this method.

  描述了一种使用碘代苯作为氧化剂从酰胺合成 1,3-二取代脲和氨基甲酸酯的简单有效的方法。对称和不对称尿素和氨基甲酸酯可以通过该程序以高达 98% 的产率制备。通过该方法也可以以良好的产率制备脲肽。
• Biocatalytic Hydrolysis of 3-Hydroxyalkanenitriles to 3-Hydroxyalkanoic Acids
  作者：Eugenia C. Hann、Amy E. Sigmund、Susan K. Fager、Frederick B. Cooling、John E. Gavagan、Arie Ben-Bassat、Sarita Chauhan、Mark S. Payne、Susan M. Hennessey、Robert DiCosimo

  DOI：10.1002/adsc.200303007

  日期：2003.6

  Microbial catalysts having a combination of nitrile hydratase and amidase activities had a significantly-higher specific activity for hydrolysis of 3-hydroxyalkanenitriles than microbial nitrilase catalysts. Comamonas testosteroni 22–1, Dietzia sp. ADL1 and Comamonas testosteroni 5-MGAM-4D nitrile hydratase/amidase biocatalysts each hydrolyzed 3-hydroxyvaleronitrile to 3-hydroxyvaleric acid (as the

  具有腈水合酶和酰胺酶活性的组合的微生物催化剂具有比微生物腈水解酶催化剂更高的水解3-羟基链烯腈的比活性。Comamonas testosteroni 22–1，Dietzia sp.。ADL1和Comamonas睾丸激素5-MGAM-4D腈水合酶/酰胺酶生物催化剂各自将3-羟基戊腈水解为3-羟基戊酸（以铵盐的形式），产率为99-100％，但是在催化剂循环的连续分批反应中，固定有藻酸盐的C睾丸激素5-MGAM-4D具有出色的酶稳定性和体积生产率。在一系列连续的85次间歇反应中，使用生物催化剂进行循环以生产1.0 M 3-羟基戊酸，最终反应中回收的腈水合酶和酰胺酶活性分别为初始活性的29％和40％。该系列反应的催化剂生产率为670 g 3-羟基戊酸/ g干细胞重量（50 g 3-羟基戊酸/ g生物催化剂珠），该系列中初始反应的体积生产率为44 g 3-HVA /升/小时 用藻酸盐固定的睾丸梭菌
• Scheibler; Magasanik, Chemische Berichte, 1915, vol. 48, p. 1812
  作者：Scheibler、Magasanik

  DOI：——

  日期：——
• A high throughput screening strategy for the assessment of nitrile-hydrolyzing activity towards the production of enantiopure β-hydroxy acids
  作者：Tracey M. Coady、Lee V. Coffey、Catherine O‘Reilly、Erica B. Owens、Claire M. Lennon

  DOI：10.1016/j.molcatb.2013.08.001

  日期：2013.12

  Nitrile hydrolysing enzymes have found wide use in the pharmaceutical industry for the production of fine chemicals. This work presents a strategy that facilitates the rapid identification of bacterial isolates demonstrating nitrile hydrolysing activity. The strategy incorporates toxicity, starvation and induction studies along with subsequent colorimetric screening for activity, further focusing the assessment towards the substrates of interest. This high-throughput strategy uses a 96 well plate system, and has enabled the rapid biocatalytic screening of 256 novel bacterial isolates towards beta-hydroxynitriles. Results demonstrate the strategy's potential to rapidly assess a variety of beta-hydroxynitriles including aliphatic, aromatic and dinitriles. A whole cell catalyst Rhodococcus erythropolis SET1 was identified and found to catalyse the hydrolysis of 3-hydroxybutyronitrile with remarkably high enantioselectivity under mild conditions, to afford (S)-3-hydroxybutyric acid in 42% yield and >99.9% ee. The biocatalytic capability of this strain including the variation of parameters such as temperature and time were further investigated and all results indicate the presence of a highly enantioselective if not enantiospecific nitrilase enzyme within the microbial whole cell. (C) 2013 Elsevier B.V. All rights reserved.