| 1612162-71-6

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物
• CAS: 1612162-71-6
• 化学式: C₅₄H₇₅N₁₂O₂₂P₃S
• 分子量: 1369.24
• InChiKey: DGFHRJWYBNCYRP-SSQOIBFVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.12
• 重原子数：
  92.0
• 可旋转键数：
  40.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  523.12
• 氢给体数：
  14.0
• 氢受体数：
  24.0

反应信息

• 作为产物：
  描述：

  coenzyme A trilithium salt 、 4-苯甲酰苯甲酸 、 溴乙酸 、 芴甲氧羰酰基-6-氨基己酸 、 Fmoc-Lys(ivDde)-OH 、 Fmoc-L-炔丙基甘氨酸 在 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 N,N-二异丙基乙胺 、 哌啶 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 2.17h， 以24%的产率得到
  参考文献：
  名称：

  Chemoproteomic Profiling of Lysine Acetyltransferases Highlights an Expanded Landscape of Catalytic Acetylation

  摘要：

  Lysine acetyltransferases (KATs) play a critical role in the regulation of gene expression, metabolism, and other key cellular functions. One shortcoming of traditional KAT assays is their inability to study KAT activity in complex settings, a limitation that hinders efforts at KAT discovery, characterization, and inhibitor development. To address this challenge, here we describe a suite of cofactor-based affinity probes capable of profiling KAT activity in biological contexts. Conversion of KAT bisubstrate inhibitors to clickable photoaffinity probes enables the selective covalent labeling of three phylogenetically distinct families of KAT enzymes. Cofactor-based affinity probes report on KAT activity in cell lysates, where KATs exist as multiprotein complexes. Chemical affinity purification and unbiased LC-MS/MS profiling highlights an expanded landscape of orphan lysine acetyltransferases present in the human genome and provides insight into the global selectivity and sensitivity of CoA-based proteomic probes that will guide future applications. Chemoproteomic profiling provides a powerful method to study the molecular interactions of KATs in native contexts and will aid investigations into the role of KATs in cell state and disease.

  DOI：

  10.1021/ja502372j