lanosterol-3-TMS | 55493-84-0

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: lanosterol-3-TMS
• 英文别名: lanosterol TMS ether；Silane, [[(3beta)-lanosta-8,24-dien-3-yl]oxy]trimethyl-；trimethyl-[[(3S,5R,10S,13R,14R,17R)-4,4,10,13,14-pentamethyl-17-[(2R)-6-methylhept-5-en-2-yl]-2,3,5,6,7,11,12,15,16,17-decahydro-1H-cyclopenta[a]phenanthren-3-yl]oxy]silane
• CAS: 55493-84-0
• 化学式: C₃₃H₅₈OSi
• 分子量: 498.908
• InChiKey: VUPPLGLOGXZZKA-OEZDDPMWSA-N

物化性质

• 保留指数：
  3327;3327

计算性质

• 辛醇/水分配系数(LogP)：
  10.34
• 重原子数：
  35
• 可旋转键数：
  6
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  9.2
• 氢给体数：
  0
• 氢受体数：
  1

反应信息

• 作为产物：
  描述：

  tert-butyl-dimethyl-[[(3S,5R,10S,13R,14R,17R)-4,4,10,13,14-pentamethyl-17-[(2R)-6-methylhept-5-en-2-yl]-2,3,5,6,7,11,12,15,16,17-decahydro-1H-cyclopenta[a]phenanthren-3-yl]oxy]silane 在 咪唑 、 四丁基氟化铵 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 为溶剂， 反应 49.0h， 生成 lanosterol-3-TMS
  参考文献：
  名称：

  WO2023/30332

  摘要：

  公开号：

文献信息

• Heterologous expression and characterization of the sterol 14α-demethylase CYP51F1 from Candida albicans
  作者：Hyoung-Goo Park、Im-Soon Lee、Young-Jin Chun、Chul-Ho Yun、Jonathan B. Johnston、Paul R. Ortiz de Montellano、Donghak Kim

  DOI：10.1016/j.abb.2011.02.002

  日期：2011.5

  Lanosterol 14 alpha-demethylase (CYP51F1) from Candida albicans is known to be an essential enzyme in fungal sterol biosynthesis. Wild-type CYP51F1 and several of its mutants were heterologously expressed in Escherichia coli, purified, and characterized. It exhibited a typical reduced CO-difference spectrum with a maximum at 446 nm. Reconstitution of CYP51F1 with NADPH-P450 reductase gave a system that successfully converted lanosterol to its demethylated product. Titration of the purified enzyme with lanosterol produced a typical type I spectral change with K-d = 6.7 mu M. The azole antifungal agents econazole, fluconazole, ketoconazole, and itraconazole bound tightly to CYP51F1 with K-d values between 0.06 and 0.42 mu M. The CYP51F1 mutations F105L, D116E, Y132H, and R467K frequently identified in clinical isolates were examined to determine their effect on azole drug binding affinity. The azole K-d values of the purified F105L, D116E, and R467K mutants were little altered. A homology model of C. albicans CYP51F1 suggested that Tyr132 in the BC loop is located close to the heme in the active site, providing a rationale for the modified heme environment caused by the Y132H substitution. Taken together, functional expression and characterization of CYP51F1 provide a starting basis for the design of agents effective against C. albicans infections. (C) 2011 Elsevier Inc. All rights reserved.