N-(2-氧代乙基)甲酰胺 | 43215-61-8

• 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
• 中文名称: N-(2-氧代乙基)甲酰胺
• 英文名称: (formylamino)acetaldehyde
• 英文别名: N-formamidoacetaldehyde；N-formylglycinal；Deoxy-glycal；N-(2-oxoethyl)formamide
• CAS: 43215-61-8
• 化学式: C₃H₅NO₂
• mdl: MFCD19219998
• 分子量: 87.0782
• InChiKey: HQJXAPWUFPJMDL-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.9
• 重原子数：
  6
• 可旋转键数：
  2
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.333
• 拓扑面积：
  46.2
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  1,3-二羟基丙酮 、 N-(2-氧代乙基)甲酰胺 在 L-rhamnulose-1-phosphate aldolase N₂₉D mutant 作用下， 反应 72.0h， 以92%的产率得到N-[(2S,3R)-2,3,5-trihydroxy-4-oxopentyl]formamide
  参考文献：
  名称：

  重新设计L-鼠李糖-1-磷酸醛缩酶对二羟基丙酮依赖性醛缩酶的磷酸结合位点

  摘要：

  据报道，由L-鼠李糖-1-磷酸醛缩酶（RhuA）（一种依赖于磷酸二羟基丙酮的醛缩酶）催化的醛基中的未磷酸化二羟基丙酮（DHA）醛缩醛加成反应。此外，RhuA野生型磷酸结合位点的单点突变，即在N29位用天冬氨酸取代天冬酰胺，使DHA与其他醛受体而不是天然L的羟醛加成反应增加了3倍。丙醛 RhuA N29D突变体修改了天然底物的最佳酶设计，并改变了其催化性能，使醛缩酶比其他添加DHA的醛缩酶更具通用性。

  DOI：

  10.1002/adsc.201000719
• 作为产物：
  描述：

  (E)-N-(3-Phenyl-2-propenyl)formamid 在 二甲基硫 、 臭氧 作用下， 生成 N-(2-氧代乙基)甲酰胺
  参考文献：
  名称：

  .alpha.-Amino aldehyde equivalents as substrates for rabbit muscle aldolase: synthesis of 1,4-dideoxy-D-arabinitol and 2(R),5(R)-bis(hydroxymethyl)-3(R),4(R)-dihydroxypyrrolidine

  摘要：

  This work examined the application of rabbit muscle aldolase (RAMA) to stereospecific carbon-carbon bond formation in the preparation of carbohydrates containing amino groups. Several alpha-amino aldehyde equivalents were evaluated as substrates for RAMA and for their synthetic utility in transformations following the aldol reaction. This methodology is illustrated by the syntheses of the pyrrolidine alkaloids 1,4-dideoxy-D-arabinitol and 2(R),5(R)-bis(hydroxymethyl)-3(R), 4(R)-dihydroxypyrrolidine. The kinetic resolution of racemic aldehydes by RAMA and mild methods for transforming the amino equivalents into the desired amines are discussed briefly.

  DOI：

  10.1021/jo00012a015

文献信息

• Stereoselective synthesis of cationic heterobidentate C(NHC)/SR rhodium(I) complexes using stereodirecting N,N-dialkylamino groups
  作者：Abel Ros、Manuel Alcarazo、David Monge、Eleuterio Álvarez、Rosario Fernández、José M. Lassaletta

  DOI：10.1016/j.tetasy.2010.04.041

  日期：2010.6

  The synthesis of two different types of chiral C/S ligands based upon N-(N,N-dialkylamino)-substituted N-heterocyclic carbenes and thioether functionalities, along with their neutral [RhCl(CNH)(COD)] and cationic [Rh(I)(NHC/S)(COD)]+ complexes, has been accomplished. (S)-2-[(Phenylthio)methyl]pyrrolidine, carrying the thioether moiety, and (2S,5S)-2,5-diphenylpyrrolidine, combined with a thioether

  基于N-（N，N-二烷基氨基）-取代的N-杂环卡宾和硫醚官能团及其中性[RhCl（CNH）（COD）]和阳离子[Rh]的两种不同类型的手性C / S配体的合成（I）（NHC / S）（COD）] +配合物已完成。（S）-2-[（（苯硫基）甲基]吡咯烷，带有硫醚部分，和（2 S，5 S）-2,5-二苯基吡咯烷与硫醚官能化的侧链结合，被作为潜在的立体定向基团进行了研究。只有后者在中性络合物的形成中提供了高选择性，从而导致新形成的，构型稳定的C（NHC）-Rh键具有单一的对映体（de> 98％）。然而，相应的阳离子型[Rh（I）（NHC / S）（COD）] +配合物的合成分别导致形成单个（R a，S S）和（S a，S S）非对映异构体，每种情况下四种可能的络合物的[[（R a / S a）C（NHC）–Rh轴与（S s / R s）通过协调形成立体异构S中心]。对于脯氨酸衍生物，（R a /
• HUNG, REBECCA R.;STRAUB, JULIE ANN;WHITESIDES, GEORGE M., J. ORG. CHEM., 56,(1991) N2, C. 3849-3855
  作者：HUNG, REBECCA R.、STRAUB, JULIE ANN、WHITESIDES, GEORGE M.

  DOI：——

  日期：——
• .alpha.-Amino aldehyde equivalents as substrates for rabbit muscle aldolase: synthesis of 1,4-dideoxy-D-arabinitol and 2(R),5(R)-bis(hydroxymethyl)-3(R),4(R)-dihydroxypyrrolidine
  作者：Rebecca R. Hung、Julie Ann Straub、George M. Whitesides

  DOI：10.1021/jo00012a015

  日期：1991.6

  This work examined the application of rabbit muscle aldolase (RAMA) to stereospecific carbon-carbon bond formation in the preparation of carbohydrates containing amino groups. Several alpha-amino aldehyde equivalents were evaluated as substrates for RAMA and for their synthetic utility in transformations following the aldol reaction. This methodology is illustrated by the syntheses of the pyrrolidine alkaloids 1,4-dideoxy-D-arabinitol and 2(R),5(R)-bis(hydroxymethyl)-3(R), 4(R)-dihydroxypyrrolidine. The kinetic resolution of racemic aldehydes by RAMA and mild methods for transforming the amino equivalents into the desired amines are discussed briefly.
• Redesign of the Phosphate Binding Site of L-Rhamnulose- 1-Phosphate Aldolase towards a Dihydroxyacetone Dependent Aldolase
  作者：Xavier Garrabou、Jesús Joglar、Teodor Parella、Ramon Crehuet、Jordi Bujons、Pere Clapés

  DOI：10.1002/adsc.201000719

  日期：2011.1.10

  The aldol addition of unphosphorylated dihydroxyacetone (DHA) to aldehydes catalyzed by L‐rhamnulose‐1‐phosphate aldolase (RhuA), a dihydroxyacetone phosphate‐dependent aldolase, is reported. Moreover, a single point mutation in the phosphate binding site of the RhuA wild type, that is, substitution of aspartate for asparagine at position N29, increased by 3‐fold the of aldol addition reactions of

  据报道，由L-鼠李糖-1-磷酸醛缩酶（RhuA）（一种依赖于磷酸二羟基丙酮的醛缩酶）催化的醛基中的未磷酸化二羟基丙酮（DHA）醛缩醛加成反应。此外，RhuA野生型磷酸结合位点的单点突变，即在N29位用天冬氨酸取代天冬酰胺，使DHA与其他醛受体而不是天然L的羟醛加成反应增加了3倍。丙醛 RhuA N29D突变体修改了天然底物的最佳酶设计，并改变了其催化性能，使醛缩酶比其他添加DHA的醛缩酶更具通用性。