| 1263056-99-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• CAS: 1263056-99-0
• 化学式: C₂₈H₄₇N₈O₁₈P
• 分子量: 814.698
• InChiKey: NKGWSFVUYWPWEX-OEGPVOQTSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -8.4
• 重原子数：
  55.0
• 可旋转键数：
  12.0
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.82
• 拓扑面积：
  431.4
• 氢给体数：
  14.0
• 氢受体数：
  24.0

反应信息

• 作为产物：
  描述：

  卡那霉素碱 、 5’-肌苷酸 在 DL-dithiothreitol 、 aminoglycoside nucleotidyltransferase from staphylococcus aureus 、 potassium chloride 、 magnesium chloride 作用下， 生成
  参考文献：
  名称：

  Dissecting the cosubstrate structure requirements of the Staphylococcus aureus aminoglycoside resistance enzyme ANT(4′)

  摘要：

  Aminoglycosides are important antibiotics used against a wide range of pathogens. As a mechanism of defense, bacteria have evolved enzymes able to inactivate these drugs by regio-selectively adding a variety of functionalities (acetyl, phospho, and nucelotidyl groups) to their scaffolds. The aminoglycoside nucleotidyltransferase ANT(4') is one of the most prevalent and unique modifying-enzymes. Here, by TLC, HRMS, and colorimetric assays, we demonstrate that the resistance enzyme ANT(4') from Staphylococcus aureus is highly substrate and cosubstrate promiscuous. We show that deoxy-ribonucleotide triphosphates (dNTPs) are better cosubstrates than NTPs. We demonstrate that the position of the triphosphate group (5' and not 3') on the ribose/deoxyribose ring is important for recognition by ANT(4'), and that NTPs with larger substituents at the 3'-position of the ribose ring are not cosubstrates for ANT(4'). We confirm that for all aminoglycosides tested, the respective nucleotidylated products are completely inactive. These results provide valuable insights into the development of strategies to combat the ever-growing bacterial resistance problem. (C) 2010 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.bbrc.2010.10.119