(R)-3-(4-Methoxy-phenyl)-4,5-dihydro-isoxazole-5-carboxylic acid | 721430-36-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 英文名称: (R)-3-(4-Methoxy-phenyl)-4,5-dihydro-isoxazole-5-carboxylic acid
• 英文别名: (5R)-3-(4-methoxyphenyl)-4,5-dihydro-1,2-oxazole-5-carboxylic acid
• CAS: 721430-36-0
• 化学式: C₁₁H₁₁NO₄
• 分子量: 221.213
• InChiKey: HSCXSJZYFWHROH-SNVBAGLBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  16
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  68.1
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  (R)-3-(4-Methoxy-phenyl)-4,5-dihydro-isoxazole-5-carboxylic acid 在 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 48.33h， 生成 (R)-3-(4-Methoxy-phenyl)-4,5-dihydro-isoxazole-5-carboxylic acid hydroxyamide
  参考文献：
  名称：

  Inhibition of the Antibacterial Target UDP-(3-O-acyl)-N-acetylglucosamine Deacetylase (LpxC):  Isoxazoline Zinc Amidase Inhibitors Bearing Diverse Metal Binding Groups

  摘要：

  UDP-3-O-[R-3-hydroxymyristoyl]-GlcNAc deacetylase (LpxC) is a zinc amidase that catalyzes the second step of lipid A biosynthesis in Gram negative bacteria. Known inhibitors of this enzyme are oxazolines incorporating a hydroxamic acid at the 4-position, which is believed to coordinate to the single essential zinc ion. A new structural class of inhibitors was designed to incorporate a more stable and more synthetically. versatile isoxazoline core. The synthetic versatility of the isoxazoline allowed for a broad study of metal binding. groups. Nine of 17 isoxazolines, each incorporating a different potential metal binding functional group, were found to exhibit enzyme inhibitory activity, including one that is more active than the corresponding hydroxamic acid. Additionally, a designed affinity label inhibits LpxC in a time-dependent manner.

  DOI：

  10.1021/jm020183v
• 作为产物：
  描述：

  (5R)-5-hydroxymethyl-3-(p-methoxyphenyl)-4,5-dihydroisoxazole 在 jones reagent 作用下， 以 丙酮 为溶剂， 反应 3.0h， 以42%的产率得到(R)-3-(4-Methoxy-phenyl)-4,5-dihydro-isoxazole-5-carboxylic acid
  参考文献：
  名称：

  Inhibition of the Antibacterial Target UDP-(3-O-acyl)-N-acetylglucosamine Deacetylase (LpxC):  Isoxazoline Zinc Amidase Inhibitors Bearing Diverse Metal Binding Groups

  摘要：

  UDP-3-O-[R-3-hydroxymyristoyl]-GlcNAc deacetylase (LpxC) is a zinc amidase that catalyzes the second step of lipid A biosynthesis in Gram negative bacteria. Known inhibitors of this enzyme are oxazolines incorporating a hydroxamic acid at the 4-position, which is believed to coordinate to the single essential zinc ion. A new structural class of inhibitors was designed to incorporate a more stable and more synthetically. versatile isoxazoline core. The synthetic versatility of the isoxazoline allowed for a broad study of metal binding. groups. Nine of 17 isoxazolines, each incorporating a different potential metal binding functional group, were found to exhibit enzyme inhibitory activity, including one that is more active than the corresponding hydroxamic acid. Additionally, a designed affinity label inhibits LpxC in a time-dependent manner.

  DOI：

  10.1021/jm020183v

文献信息

• Inhibition of the Antibacterial Target UDP-(3-<i>O</i>-acyl)-<i>N</i>-acetylglucosamine Deacetylase (LpxC):  Isoxazoline Zinc Amidase Inhibitors Bearing Diverse Metal Binding Groups
  作者：Michael C. Pirrung、L. Nathan Tumey、Christian R. H. Raetz、Jane E. Jackman、Karnem Snehalatha、Amanda L. McClerren、Carol A. Fierke、Stephanie L. Gantt、Kristin M. Rusche

  DOI：10.1021/jm020183v

  日期：2002.9.1

  UDP-3-O-[R-3-hydroxymyristoyl]-GlcNAc deacetylase (LpxC) is a zinc amidase that catalyzes the second step of lipid A biosynthesis in Gram negative bacteria. Known inhibitors of this enzyme are oxazolines incorporating a hydroxamic acid at the 4-position, which is believed to coordinate to the single essential zinc ion. A new structural class of inhibitors was designed to incorporate a more stable and more synthetically. versatile isoxazoline core. The synthetic versatility of the isoxazoline allowed for a broad study of metal binding. groups. Nine of 17 isoxazolines, each incorporating a different potential metal binding functional group, were found to exhibit enzyme inhibitory activity, including one that is more active than the corresponding hydroxamic acid. Additionally, a designed affinity label inhibits LpxC in a time-dependent manner.