oceanapiside

• 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: oceanapiside
• 英文别名: (2S,3R,26R,27R)-2,27-diamino-1,26-dihydroxy-3-[(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydropyran-2-yl]oxy-octacosan-13-one；(2S,3R,26R,27R)-2,27-diamino-1,26-dihydroxy-3-[(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoctacosan-13-one
• 化学式: C₃₄H₆₈N₂O₉
• 分子量: 648.922
• InChiKey: XJGZZDLCVLWEBE-LBAMHCMXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.1
• 重原子数：
  45
• 可旋转键数：
  29
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.97
• 拓扑面积：
  209
• 氢给体数：
  8
• 氢受体数：
  11

反应信息

• 作为反应物：
  描述：

  oceanapiside 在 盐酸 作用下， 以 甲醇 为溶剂， 反应 24.0h， 生成 oceanapiside aglycon
  参考文献：
  名称：

  Inhibition and kinetics of mycobacterium tuberculosis and mycobacterium smegmatis mycothiol-S-conjugate amidase by natural product inhibitors

  摘要：

  The current rise in mycobacterial-related infections and disease, coupled with drug resistance, underlines the continuing need for new antimycobacterials. To this end, we have screened similar to1500 extracts derived from marine plants and invertebrates and terrestrial fungi for their ability to inhibit a newly described mycobacterial detoxification enzyme mycothiol-S-conjugate amidase (MCA). As described in this paper, our screening and chemistry efforts thus far have led to the identification of 13 natural product inhibitors that represent six different structural classes. By conducting enzyme inhibition assays using varied inhibitor and substrate concentrations, we have determined the mode of inhibition of Mycobacterium tuberculosis MCA for four of these compounds. We show that two types of bromo tyro sine-derived natural products are competitive inhibitors of MCA; while oceanapiside, an alpha,omega-bisaminohydroxy glycosphingolipid, and the fungal metabolite gliotoxin, a dithiadiketopiperazine, are simple and mixed non-competitive inhibitors, respectively. Correlation of these results with the chemical structures suggests that MCA is a metalloenzyme and that the oximinoamide and spiro-isoxazoline amide groups present in the competitive inhibitors are substrate mimics. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(02)00345-0

文献信息

• Inhibition and kinetics of mycobacterium tuberculosis and mycobacterium smegmatis mycothiol-S-conjugate amidase by natural product inhibitors
  作者：Gillian M. Nicholas、Lisa L. Eckman、Gerald L. Newton、Robert C. Fahey、Satyajit Ray、Carole A. Bewley

  DOI：10.1016/s0968-0896(02)00345-0

  日期：2003.2

  The current rise in mycobacterial-related infections and disease, coupled with drug resistance, underlines the continuing need for new antimycobacterials. To this end, we have screened similar to1500 extracts derived from marine plants and invertebrates and terrestrial fungi for their ability to inhibit a newly described mycobacterial detoxification enzyme mycothiol-S-conjugate amidase (MCA). As described in this paper, our screening and chemistry efforts thus far have led to the identification of 13 natural product inhibitors that represent six different structural classes. By conducting enzyme inhibition assays using varied inhibitor and substrate concentrations, we have determined the mode of inhibition of Mycobacterium tuberculosis MCA for four of these compounds. We show that two types of bromo tyro sine-derived natural products are competitive inhibitors of MCA; while oceanapiside, an alpha,omega-bisaminohydroxy glycosphingolipid, and the fungal metabolite gliotoxin, a dithiadiketopiperazine, are simple and mixed non-competitive inhibitors, respectively. Correlation of these results with the chemical structures suggests that MCA is a metalloenzyme and that the oximinoamide and spiro-isoxazoline amide groups present in the competitive inhibitors are substrate mimics. (C) 2002 Elsevier Science Ltd. All rights reserved.