N-(2-azido-3-oxo-propyl)-acetamide | 957796-70-2

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: N-(2-azido-3-oxo-propyl)-acetamide
• 英文别名: 3-Azido-2-acetamidopropanal；N-(2-azido-3-oxopropyl)acetamide
• CAS: 957796-70-2
• 化学式: C₅H₈N₄O₂
• 分子量: 156.144
• InChiKey: MMMYHNNYSAXDMR-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.2
• 重原子数：
  11
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.6
• 拓扑面积：
  60.5
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  N-(2-azido-3-oxo-propyl)-acetamide 在 盐酸 、 三羟甲基氨基甲烷 、 sodium chloride 作用下， 以 水 为溶剂， 反应 2.0h， 生成 N-((2R,3R,4S)-2-Azido-3,4,6-trihydroxy-5-oxo-hexyl)-acetamide
  参考文献：
  名称：

  Inhibition of N-acetylglucosaminyl transfer enzymes: chemical-enzymic synthesis of new five-membered acetamido azasugars

  摘要：

  Two new acetamido azasugars have been synthesized and tested as inhibitors of beta-N-acetylglucosaminase. Ozonolysis of enantiomerically pure N-(4-phenyl-2-azido-3-butenyl)acetamide, derived from cinnamic aldehyde, followed by lipase-catalyzed resolution of the amine intermediate 5, gave 2-azido-3-acetamidopropanal which was then condensed with dihydroxyacetone phosphate by using FDP-aldolase. The condensed product was dephosphorylated and hydrogenated to afford the five-membered acetamido azasugar analogous to N-acetylglucosamine. Compounds 1 and 2 prepared in this manner were new competitive inhibitors of a beta-N-acetylglucosaminidase with K(i) values of 1.9 and 3.6 muM, respectively, and could be useful for the synthesis of N-acetylglucosaminyltransferase inhibitors.

  DOI：

  10.1021/jo00070a013
• 作为产物：
  描述：

  (E)-1-(N-乙酰氨基)氨基-2-叠氮基-4-苯基-3-丁烯 在 臭氧 、 二甲基硫 作用下， 以 甲醇 为溶剂， 反应 24.0h， 生成 N-(2-azido-3-oxo-propyl)-acetamide
  参考文献：
  名称：

  Iminocyclitol inhibitors of hexoaminidase and glycosidase

  摘要：

  披露了设计的亚氨基糖醇，它们对己糖苷酶和苷具有强大的抑制活性。

  公开号：

  US06774140B1

文献信息

• Borate as a Phosphate Ester Mimic in Aldolase-Catalyzed Reactions: Practical Synthesis ofL-Fructose andL-Iminocyclitols
  作者：Masakazu Sugiyama、Zhangyong Hong、Lisa J. Whalen、William A. Greenberg、Chi-Huey Wong

  DOI：10.1002/adsc.200600356

  日期：2006.12

  Dihydroxyacetone phosphate (DHAP)-dependent aldolases have been widely used for the organic synthesis of unnatural sugars or derivatives. The practicality of using DHAP-dependent aldolases is limited by their strict substrate specificity and the high cost and instability of DHAP. Here we report that the DHAP-dependent aldolase L-rhamnulose 1-phosphate aldolase (RhaD) accepts dihydroxyacetone (DHA)

  磷酸二羟基丙酮（DHAP）依赖性醛缩酶已广泛用于非天然糖或衍生物的有机合成。使用依赖DHAP的醛缩酶的实用性受到其严格的底物特异性以及DHAP的高成本和不稳定性的限制。在这里我们报告依赖DHAP的醛缩酶L-鼠李糖1-磷酸醛缩酶（RhaD）在硼酸盐缓冲液的存在下接受二羟基丙酮（DHA）作为供体底物，大概是通过原位可逆的形成DHA硼酸酯。该反应似乎是不可逆的，热力学上将产物捕获为硼酸盐配合物。我们已经将该发现用于开发非热量甜味剂L-果糖的实用一步合成。在RhaD存在下，由消旋甘油醛和DHA合成L-果糖，硼酸盐的克收率为92％。我们还分两步合成了一系列L-亚氨基环糖醇，它们是潜在的糖苷酶抑制剂。
• <scp>d</scp>-Fructose-6-Phosphate Aldolase-Catalyzed One-Pot Synthesis of Iminocyclitols
  作者：Masakazu Sugiyama、Zhangyong Hong、Pi-Hui Liang、Stephen M. Dean、Lisa J. Whalen、William A. Greenberg、Chi-Huey Wong

  DOI：10.1021/ja073911i

  日期：2007.11.28

  A one-pot chemoenzymatic method for the synthesis of a variety of new iminocyclitols from readily available, non-phosphorylated donor substrates has been developed. The method utilizes the recently discovered fructose-6-phosphate aldolase (FSA), which is functionally distinct from known aldolases in its tolerance of different donor substrates as well as acceptor substrates. Kinetic studies were performed with dihydroxyacetone (DHA), the presumed endogenous substrate for FSA, as well as hydroxy acetone (HA) and 1-hydroxy-2-butanone (HB) as donor substrates, in each case using glyceraidehyde-3-phosphate as acceptor substrate. Remarkably, FSA used the three donor substrates with equal efficiency, with k(cat)/K-M-values of 33, 75, and 20 M-1 s(-1), respectively. This level of donor substrate tolerance is unprecedented for an aldolase. Furthermore, DHA, HA, and HB were accepted as donors in FSA-catalyzed aldol reactions with a variety of azido- and Cbz-amino aldehyde acceptors. The broad substrate tolerance of FSA and the ability to circumvent the need for phosphorylated substrates allowed for one-pot synthesis of a number of known and novel iminocyclitols in good yields, and in a very concise fashion. New iminocyclitols were assayed as inhibitors against a panel of glycosidases. Compounds 15 and 16 were specific alpha-mannosidase inhibitors, and 24 and 26 were potent and selective inhibitors of beta-N-acetylglucosaminidases in the submicromolar range. Facile access to these compounds makes them attractive core structures for further inhibitor optimization.