2-hydroxy-6-(hydroxyimino)-5-pentanamidohexane-1,3,4-tripentanoate | 885330-96-1

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: 2-hydroxy-6-(hydroxyimino)-5-pentanamidohexane-1,3,4-tripentanoate
• CAS: 885330-96-1
• 化学式: C₂₆H₄₆N₂O₉
• 分子量: 530.659
• InChiKey: BERDVVGJJNBESQ-BLNVZXSVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.42
• 重原子数：
  37.0
• 可旋转键数：
  21.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.81
• 拓扑面积：
  160.82
• 氢给体数：
  3.0
• 氢受体数：
  10.0

反应信息

• 作为反应物：
  描述：

  2-hydroxy-6-(hydroxyimino)-5-pentanamidohexane-1,3,4-tripentanoate 在 N-氯代丁二酰亚胺 、 1,8-二氮杂双环[5.4.0]十一碳-7-烯 、 三乙胺 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 1.5h， 生成 5-pentanamido-2-(pentanoyloxymethyl)-6-(phenylcarbamoyloxyimino)tetrahydro-2H-pyran-3,4-dipentanoate
  参考文献：
  名称：

  An O-GlcNAcase-Specific Inhibitor and Substrate Engineered by the Extension of the N-Acetyl Moiety

  摘要：

  A novel analogue of PUGNAc, a potent O-GlcNAcase inhibitor, was synthesized and analyzed as an inhibitor of O-GlcNAcase, hexosaminidase A, and hexosaminidase B. While PUGNAc does not demonstrate selective inhibition of these related enzymes, the extension of the acetyl moiety to the longer butyl chain provided a compound with depressed inhibition of O-GlcNAcase and no observed inhibition of either hexosaminidase A or hexosaminidase B. Further, we applied this knowledge of substrate recognition at the N-acetyl group to our recently reported fluorogenic substrate for monitoring O-GlcNAcase activity. Gratifyingly, this altered small molecule was demonstrated to be a potent substrate for O-GlcNAcase while possessing no activity at hexosaminidase A. This reagent provides, for the first time, a means for monitoring O-GlcNAcase activity independent of the related enzymes hexosaminidase A and hexosaminidase B.

  DOI：

  10.1021/ja0582915
• 作为产物：
  描述：

  在 吡啶 、 盐酸羟胺 、 碳酸氢铵 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 反应 11.0h， 生成 2-hydroxy-6-(hydroxyimino)-5-pentanamidohexane-1,3,4-tripentanoate
  参考文献：
  名称：

  An O-GlcNAcase-Specific Inhibitor and Substrate Engineered by the Extension of the N-Acetyl Moiety

  摘要：

  A novel analogue of PUGNAc, a potent O-GlcNAcase inhibitor, was synthesized and analyzed as an inhibitor of O-GlcNAcase, hexosaminidase A, and hexosaminidase B. While PUGNAc does not demonstrate selective inhibition of these related enzymes, the extension of the acetyl moiety to the longer butyl chain provided a compound with depressed inhibition of O-GlcNAcase and no observed inhibition of either hexosaminidase A or hexosaminidase B. Further, we applied this knowledge of substrate recognition at the N-acetyl group to our recently reported fluorogenic substrate for monitoring O-GlcNAcase activity. Gratifyingly, this altered small molecule was demonstrated to be a potent substrate for O-GlcNAcase while possessing no activity at hexosaminidase A. This reagent provides, for the first time, a means for monitoring O-GlcNAcase activity independent of the related enzymes hexosaminidase A and hexosaminidase B.

  DOI：

  10.1021/ja0582915