3alpha,7alpha-dihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA(4-)

• 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: 3alpha,7alpha-dihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA(4-)
• 英文别名: [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-2-[[[[(3R)-4-[[3-[2-[(6R)-6-[(3R,5S,7R,8R,9S,10S,13R,14S,17R)-3,7-dihydroxy-10,13-dimethyl-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]-2-methyl-3-oxoheptanoyl]sulfanylethylamino]-3-oxopropyl]amino]-3-hydroxy-2,2-dimethyl-4-oxobutoxy]-oxidophosphoryl]oxy-oxidophosphoryl]oxymethyl]-4-hydroxyoxolan-3-yl] phosphate
• 化学式: C48H74N7O20P3S-4
• 分子量: 1194.1
• InChiKey: QWTJBRPOHKIMDT-MVFHLHSISA-J

计算性质

• 辛醇/水分配系数(LogP)：
  -0.4
• 重原子数：
  79
• 可旋转键数：
  25
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.81
• 拓扑面积：
  458
• 氢给体数：
  7
• 氢受体数：
  25

反应信息

• 作为产物：
  描述：

  (24R,25R)-3alpha,7alpha,24-trihydroxy-5beta-cholestan-26-oyl-CoA(4-) 、 nicotinamide adenine dinucleotide 生成 3alpha,7alpha-dihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA(4-) 、 氢(+1)阳离子 、 NADH
  参考文献：
  名称：

  Conjugation reactions catalyzed by bifunctional proteins related to β-oxidation in bile acid biosynthesis

  摘要：

  The conjugation reactions of hydration and dehydrogenation catalyzed by the dehydratase and dehydrogenase activities of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein (DBP) and enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase bifunctional protein (LBP) in the side chain degradation step of bile acid biosynthesis were investigated using chemically synthesized C-27-bile acid CoA esters as substrates. The hydration catalyzed by DBP showed high diastereoselectivity for (24E)-3 alpha ,7 alpha ,12 alpha -trihydroxy- and (24E)-3 alpha ,7 alpha -dihydroxy-5 beta -cholest-24-en-26-oyl CoA to give (24R,25R)-3 alpha ,7 alpha ,12 alpha ,24-tetrahydroxy- and (24R, 25R)-3 alpha ,7 alpha ,24-trihydroxy-5 beta -cholestan-26-oyl CoAs, respectively, and the dehydrogenation catalyzed by DBP also showed high stereospecificity for the above (24R,25R)-isomers to give 3 alpha ,7 alpha ,12 alpha -trihydroxy- and 3 alpha ,7 alpha -dihydroxy-24-oxo-5 beta -cholestan-26-oyl CoAs, respectively. On the other hand, the dehydratase activity of LBP displayed a different diastereoselectivity producing the (24S,25S)-isomer, and dehydrogenase activity of LBP was stereospecific for the (24S,25R)-isomer to give the above 24-oxo-derivative. The hydration and dehydrogenation reactions catalyzed by DBP were effectively conjugated to convert (24E)-5 beta -cholestenoyl CoA to 24-oxo-5 beta -cholestanoyl CoA. However, the reactions catalyzed by LBP were not conjugated. These results indicate that DBP plays an important role in the biosynthesis of bile acid. (C) 2001 Elsevier Science Inc. All rights reserved.

  DOI：

  10.1016/s0039-128x(00)00217-8

文献信息

• Conjugation reactions catalyzed by bifunctional proteins related to β-oxidation in bile acid biosynthesis
  作者：Takao Kurosawa、Masahiro Sato、Hiroyuki Nakano、Masato Fujiwara、Tsuyoshi Murai、Teruki Yoshimura、Takashi Hashimoto

  DOI：10.1016/s0039-128x(00)00217-8

  日期：2001.1

  The conjugation reactions of hydration and dehydrogenation catalyzed by the dehydratase and dehydrogenase activities of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein (DBP) and enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase bifunctional protein (LBP) in the side chain degradation step of bile acid biosynthesis were investigated using chemically synthesized C-27-bile acid CoA esters as substrates. The hydration catalyzed by DBP showed high diastereoselectivity for (24E)-3 alpha ,7 alpha ,12 alpha -trihydroxy- and (24E)-3 alpha ,7 alpha -dihydroxy-5 beta -cholest-24-en-26-oyl CoA to give (24R,25R)-3 alpha ,7 alpha ,12 alpha ,24-tetrahydroxy- and (24R, 25R)-3 alpha ,7 alpha ,24-trihydroxy-5 beta -cholestan-26-oyl CoAs, respectively, and the dehydrogenation catalyzed by DBP also showed high stereospecificity for the above (24R,25R)-isomers to give 3 alpha ,7 alpha ,12 alpha -trihydroxy- and 3 alpha ,7 alpha -dihydroxy-24-oxo-5 beta -cholestan-26-oyl CoAs, respectively. On the other hand, the dehydratase activity of LBP displayed a different diastereoselectivity producing the (24S,25S)-isomer, and dehydrogenase activity of LBP was stereospecific for the (24S,25R)-isomer to give the above 24-oxo-derivative. The hydration and dehydrogenation reactions catalyzed by DBP were effectively conjugated to convert (24E)-5 beta -cholestenoyl CoA to 24-oxo-5 beta -cholestanoyl CoA. However, the reactions catalyzed by LBP were not conjugated. These results indicate that DBP plays an important role in the biosynthesis of bile acid. (C) 2001 Elsevier Science Inc. All rights reserved.