2-甲基-2-丙基[1-羟基-2-(羟基甲基)-3-丁炔-2-基]氨基甲酸酯 | 364631-69-6

• 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: 2-甲基-2-丙基[1-羟基-2-(羟基甲基)-3-丁炔-2-基]氨基甲酸酯
• 英文名称: Tert-butyl N-(2-ethynyl-1,3-dihydroxypropan-2-YL)carbamate
• 英文别名: tert-butyl N-[1-hydroxy-2-(hydroxymethyl)but-3-yn-2-yl]carbamate
• CAS: 364631-69-6
• 化学式: C₁₀H₁₇NO₄
• 分子量: 215.249
• InChiKey: QMBZHBUHZSXOKK-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.5
• 重原子数：
  15
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.7
• 拓扑面积：
  78.8
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  2-甲基-2-丙基[1-羟基-2-(羟基甲基)-3-丁炔-2-基]氨基甲酸酯 在 咪唑 、 4-二甲氨基吡啶 、 phosphate buffer 、 pig liver esterase 作用下， 以 吡啶 、 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 反应 27.0h， 生成 acetic acid 2-tert-butoxycarbonylamino-2-(tert-butyl-dimethyl-silanyloxymethyl)-but-3-ynyl ester
  参考文献：
  名称：

  Stereoselective Synthesis of Conformationally Constrained Glycosylated Amino Acids Using an Enzyme-Catalyzed Desymmetrization

  摘要：

  As part of an effort to probe the mechanism by which glycosyltransferases recognize glycoproteins and assemble the core structures of O-linked oligosaccharides, constrained glycopeptides, compounds 2 and 3, based on the alpha-N-acetylgalactosaminyl serine substructure 1, were designed. In this paper we describe a stereoselective preparation of protected versions of these compounds. A pig liver esterase-catalyzed enzymatic desymmetrization of a diacetate substrate, 10, was employed as a key component in the synthesis.

  DOI：

  10.1021/jo020532t
• 作为产物：
  描述：

  (5-甲酰基-2,2-二甲基-1,3-二氧六环-5-基)氨基甲酸叔丁酯 在 甲基锂 、 对甲苯磺酸 、 三乙胺 、 lithium diisopropyl amide 作用下， 以 四氢呋喃 、 甲醇 、 乙醚 、 二氯甲烷 为溶剂， 反应 31.75h， 生成 2-甲基-2-丙基[1-羟基-2-(羟基甲基)-3-丁炔-2-基]氨基甲酸酯
  参考文献：
  名称：

  New design concepts for constraining glycosylated amino acids

  摘要：

  In an effort to probe the mechanism by which glycosyltransferases recognize glycoproteins and assemble the core structures of O-linked oligosaccharides, two constrained glycopeptides based on the alpha -N-acetylgalactosaminyl serine substructure were chosen for synthesis. These compounds representing one of the two possible gauche conformations of the D-serine and L-serine configurations of the parent substructure were successfully prepared in reasonable overall yield through a convergent strategy. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0040-4020(01)00545-2

文献信息

• New design concepts for constraining glycosylated amino acids
  作者：Jonathan W Lane、Randall L Halcomb

  DOI：10.1016/s0040-4020(01)00545-2

  日期：2001.7

  In an effort to probe the mechanism by which glycosyltransferases recognize glycoproteins and assemble the core structures of O-linked oligosaccharides, two constrained glycopeptides based on the alpha -N-acetylgalactosaminyl serine substructure were chosen for synthesis. These compounds representing one of the two possible gauche conformations of the D-serine and L-serine configurations of the parent substructure were successfully prepared in reasonable overall yield through a convergent strategy. (C) 2001 Elsevier Science Ltd. All rights reserved.
• Stereoselective Synthesis of Conformationally Constrained Glycosylated Amino Acids Using an Enzyme-Catalyzed Desymmetrization
  作者：Jonathan W. Lane、Randall L. Halcomb

  DOI：10.1021/jo020532t

  日期：2003.2.1

  As part of an effort to probe the mechanism by which glycosyltransferases recognize glycoproteins and assemble the core structures of O-linked oligosaccharides, constrained glycopeptides, compounds 2 and 3, based on the alpha-N-acetylgalactosaminyl serine substructure 1, were designed. In this paper we describe a stereoselective preparation of protected versions of these compounds. A pig liver esterase-catalyzed enzymatic desymmetrization of a diacetate substrate, 10, was employed as a key component in the synthesis.