ethyl-3-[(tert-butylsulfinyl)amino]-2,2-difluoro-3-phenylpropanoate | 479480-53-0

• 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: ethyl-3-[(tert-butylsulfinyl)amino]-2,2-difluoro-3-phenylpropanoate
• 英文别名: ethyl 3-[[(R)-tert-butylsulfinyl]amino]-2,2-difluoro-3-phenylpropanoate
• CAS: 479480-53-0
• 化学式: C₁₅H₂₁F₂NO₃S
• 分子量: 333.399
• InChiKey: SAALFHDKHDZPOO-QUBVVNMWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  22
• 可旋转键数：
  8
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  74.6
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  ethyl-3-[(tert-butylsulfinyl)amino]-2,2-difluoro-3-phenylpropanoate 在 盐酸 、 methyloxirane 作用下， 以 异丙醇 为溶剂， 生成 (S)-3-amino-2,2-difluoro-3-phenylpropanoic acid 、 (S)-3-amino-2,2-difluoro-3-phenylpropanoic acid
  参考文献：
  名称：

  Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM

  摘要：

  The synthesis and evaluation of two classes of inhibitors for SgTAM, a 4-methylideneimidazole-5-one (MIO) containing tyrosine aminomutase, are described. A mechanism-based strategy was used to design analogs that mimic the substrate or product of the reaction and form covalent interactions with the enzyme through the MIO prosthetic group. The analogs were characterized by measuring inhibition constants and X-ray crystallographic structural analysis of the co-complexes bound to the aminomutase, SgTAM.

  DOI：

  10.1016/j.bmcl.2007.11.046
• 作为产物：
  描述：

  二氟溴乙酸乙酯 、 (R,E)-2-methyl-N-(phenylmethylene)-2-propanesulfinamide 在 锌 作用下， 以 四氢呋喃 为溶剂， 生成 ethyl-3-[(tert-butylsulfinyl)amino]-2,2-difluoro-3-phenylpropanoate
  参考文献：
  名称：

  Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM

  摘要：

  The synthesis and evaluation of two classes of inhibitors for SgTAM, a 4-methylideneimidazole-5-one (MIO) containing tyrosine aminomutase, are described. A mechanism-based strategy was used to design analogs that mimic the substrate or product of the reaction and form covalent interactions with the enzyme through the MIO prosthetic group. The analogs were characterized by measuring inhibition constants and X-ray crystallographic structural analysis of the co-complexes bound to the aminomutase, SgTAM.

  DOI：

  10.1016/j.bmcl.2007.11.046

文献信息

• Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM
  作者：Timothy J. Montavon、Carl V. Christianson、Grace M. Festin、Ben Shen、Steven D. Bruner

  DOI：10.1016/j.bmcl.2007.11.046

  日期：2008.5

  The synthesis and evaluation of two classes of inhibitors for SgTAM, a 4-methylideneimidazole-5-one (MIO) containing tyrosine aminomutase, are described. A mechanism-based strategy was used to design analogs that mimic the substrate or product of the reaction and form covalent interactions with the enzyme through the MIO prosthetic group. The analogs were characterized by measuring inhibition constants and X-ray crystallographic structural analysis of the co-complexes bound to the aminomutase, SgTAM.