3alpha,7alpha,12alpha-Trihydroxy-5alpha-cholan-24-yl sulfate(1-)

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 类固醇和类固醇衍生物
• 英文名称: 3alpha,7alpha,12alpha-Trihydroxy-5alpha-cholan-24-yl sulfate(1-)
• 英文别名: [(4R)-4-[(3R,5R,7R,8R,9S,10S,12S,13R,14S,17R)-3,7,12-trihydroxy-10,13-dimethyl-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]pentyl] sulfate
• 化学式: C24H41O7S-
• 分子量: 473.6
• InChiKey: BKZKSSHAWFCVDU-JLIFGLSWSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  3.3
• 重原子数：
  32
• 可旋转键数：
  5
• 环数：
  4.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  136
• 氢给体数：
  3
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  PAPS 、 七鳃鳗醇 生成 3alpha,7alpha,12alpha-Trihydroxy-5alpha-cholan-24-yl sulfate(1-) 、 Adenosine 3',5'-bismonophosphate(4-) 、 氢(+1)阳离子
  参考文献：
  名称：

  Isolation, partial purification, and characterization of a novel petromyzonol sulfotransferase from Petromyzon marinus (lamprey) larval liver

  摘要：

  We have isolated, partially purified, and characterized the 5alpha-petromyzonol (5alpha-PZ), (5alpha-cholan- 3alpha, 7alpha, 12alpha, 24-tetrahydroxy-) sulfotransferase (PZ-SULT) from larval lamprey liver. Crude liver extracts exhibited a PZ-SULT activity of 0.9120 pmol/min/mg in juvenile and 12.62 pmol/min/mg in larvae. Using crude larval liver extracts and various 5 beta-cholan substrates and allocholic acid there was negligible activity, however, with 5alpha-PZ and 3-keto-5alpha-PZ the SULT activity was 231.5 pmol/min/mg and 180.8 pmol/min/mg respectively. This established that the sulfotransferase of lamprey larval liver extracts prefers (5 alpha) substrates and it is selective for hydroxyl at C-24. PZ-SULT was purified through various chromatography procedures. Partially purified PZ-SULT exhibited a pH optimum of 8.0, a temperature optimum of 22degreesC, and activity was linear for 1h. PZ-SULT exhibited a K-m of 2.5 muM for PAPS and a K-m of 8 muM for PZ. The affinity purified peak PZ-SULT exhibited a specific activity of 2,038 pmol/min/mg. The peak protein upon SDS-PAGE, correlated to an Mw 47 kDa. Photoaffinity labeling with PAP(35)S, specifically crosslinked the 47 kDa protein, further confirming the identity of PZ-SULT. Partial amino acid sequencing of the putative 47 kDa PZ-SULT protein yielded a peptide sequence (M)SISQAVDAAFXEI, which possessed an overall (similar to35-40%) homology with mammalian SULT2B1a.-Venkatachalam, K. V., D. E. Llanos, K. J. Karami, and V. A. Malinovskii. Isolation, partial purification, and characterization of a novel petromyzonol sulfotransferase from Petromyzon marinus (lamprey) larval liver.

  DOI：

  10.1194/jlr.m300346-jlr200

文献信息

• Isolation, partial purification, and characterization of a novel petromyzonol sulfotransferase from Petromyzon marinus (lamprey) larval liver
  作者：K.V. Venkatachalam、Domingo E. Llanos、Kristophe J. Karami、Vladimir A. Malinovskii

  DOI：10.1194/jlr.m300346-jlr200

  日期：2004.3

  We have isolated, partially purified, and characterized the 5alpha-petromyzonol (5alpha-PZ), (5alpha-cholan- 3alpha, 7alpha, 12alpha, 24-tetrahydroxy-) sulfotransferase (PZ-SULT) from larval lamprey liver. Crude liver extracts exhibited a PZ-SULT activity of 0.9120 pmol/min/mg in juvenile and 12.62 pmol/min/mg in larvae. Using crude larval liver extracts and various 5 beta-cholan substrates and allocholic acid there was negligible activity, however, with 5alpha-PZ and 3-keto-5alpha-PZ the SULT activity was 231.5 pmol/min/mg and 180.8 pmol/min/mg respectively. This established that the sulfotransferase of lamprey larval liver extracts prefers (5 alpha) substrates and it is selective for hydroxyl at C-24. PZ-SULT was purified through various chromatography procedures. Partially purified PZ-SULT exhibited a pH optimum of 8.0, a temperature optimum of 22degreesC, and activity was linear for 1h. PZ-SULT exhibited a K-m of 2.5 muM for PAPS and a K-m of 8 muM for PZ. The affinity purified peak PZ-SULT exhibited a specific activity of 2,038 pmol/min/mg. The peak protein upon SDS-PAGE, correlated to an Mw 47 kDa. Photoaffinity labeling with PAP(35)S, specifically crosslinked the 47 kDa protein, further confirming the identity of PZ-SULT. Partial amino acid sequencing of the putative 47 kDa PZ-SULT protein yielded a peptide sequence (M)SISQAVDAAFXEI, which possessed an overall (similar to35-40%) homology with mammalian SULT2B1a.-Venkatachalam, K. V., D. E. Llanos, K. J. Karami, and V. A. Malinovskii. Isolation, partial purification, and characterization of a novel petromyzonol sulfotransferase from Petromyzon marinus (lamprey) larval liver.