N-(2-(3'-(4,5-dihydroxy-6-(hydroxymethyl)-3-pentanamidotetrahydro-2H-pyran-2-yloxy)-3-oxo-3H-spiro[isobenzofuran1,9'-xanthene]-6'-yloxy)-4,5-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)pentanamide | 885330-94-9

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: N-(2-(3'-(4,5-dihydroxy-6-(hydroxymethyl)-3-pentanamidotetrahydro-2H-pyran-2-yloxy)-3-oxo-3H-spiro[isobenzofuran1,9'-xanthene]-6'-yloxy)-4,5-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)pentanamide
• 英文别名: N-[(2S,3R,4R,5S,6R)-2-[6'-[(2S,3R,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-(pentanoylamino)oxan-2-yl]oxy-3-oxospiro[2-benzofuran-1,9'-xanthene]-3'-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)oxan-3-yl]pentanamide
• CAS: 885330-94-9
• 化学式: C₄₂H₅₀N₂O₁₅
• 分子量: 822.863
• InChiKey: JFZBBIXYJOCLIM-LIRWOOKWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.6
• 重原子数：
  59
• 可旋转键数：
  14
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  252
• 氢给体数：
  8
• 氢受体数：
  15

反应信息

• 作为反应物：
  描述：

  N-(2-(3'-(4,5-dihydroxy-6-(hydroxymethyl)-3-pentanamidotetrahydro-2H-pyran-2-yloxy)-3-oxo-3H-spiro[isobenzofuran1,9'-xanthene]-6'-yloxy)-4,5-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)pentanamide 在 protein O-GlcNAcase 水 作用下， 生成
  参考文献：
  名称：

  O-GlcNAcase-specific inhibitor and substrate engineered by the extension of the N-Acetyl moiety

  摘要：

  一种O-GlcNAcase特异性抑制剂和底物是通过扩展O-(2-乙酰胺基-2-脱氧-D-葡萄糖吡喃糖苷)氨基-N-苯基氨基甲酸酯（PUGNAc）的N-乙酰基部分来设计的。该试剂底物包括一个荧光团和抑制剂。这种试剂底物用于细胞内高通量分析O-GlcNAcase并且是O-GlcNAcase体内分析的成像剂。

  公开号：

  US20080182805A1
• 作为产物：
  描述：

  荧光素 在 吡啶 、 氨 、 silver(l) oxide 作用下， 以 甲醇 、 乙腈 为溶剂， 反应 51.0h， 生成 N-(2-(3'-(4,5-dihydroxy-6-(hydroxymethyl)-3-pentanamidotetrahydro-2H-pyran-2-yloxy)-3-oxo-3H-spiro[isobenzofuran1,9'-xanthene]-6'-yloxy)-4,5-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)pentanamide
  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