(3S,4S,5S)-3,4,5,7-Tetrakis-benzyloxy-1,1-dichloro-heptane-2,6-dione | 244226-71-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: (3S,4S,5S)-3,4,5,7-Tetrakis-benzyloxy-1,1-dichloro-heptane-2,6-dione
• 英文别名: (3S,4S,5S)-1,1-dichloro-3,4,5,7-tetrakis(phenylmethoxy)heptane-2,6-dione
• CAS: 244226-71-9
• 化学式: C₃₅H₃₄Cl₂O₆
• 分子量: 621.557
• InChiKey: ZCLXYMVYVMPVJV-SXLOSVNLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.6
• 重原子数：
  43
• 可旋转键数：
  18
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.26
• 拓扑面积：
  71.1
• 氢给体数：
  0
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  (3S,4S,5S)-3,4,5,7-Tetrakis-benzyloxy-1,1-dichloro-heptane-2,6-dione 在 18-冠醚-6 、 sodium acetate 作用下， 以 甲苯 为溶剂， 反应 72.0h， 生成 (2S,3S,4S,5S)-2,3,4-tri-O-benzyl-5-C-<(benzyloxy)methyl>-6,6-dichloro-1-oxo-2,3,4,5-cyclohexanetetrol 、 (2S,3S,4S,5R)-2,3,4-tri-O-benzyl-5-C-<(benzyloxy)methyl>-6,6-dichloro-1-oxo-2,3,4,5-cyclohexanetetrol
  参考文献：
  名称：

  Biosynthetic Studies on the α-Glucosidase Inhibitor Acarbose in Actinoplanes sp.:  2-epi-5-epi-Valiolone Is the Direct Precursor of the Valienamine Moiety

  摘要：

  The biosynthetic pathway leading to the mC(7)N cyclitol (valienamine) moiety of acarbose (1) in Actinoplanes sp. strain SN 223/29 has been studied using H-3-, H-2-, and C-13-labeled cyclitols. These precursors were synthesized from D-glucose or D-mannose as starting materials. The feeding experiments demonstrated that cyclitols having the same stereochemistry at C-2 as the valienamine moiety of acarbose; i.e., valienone, valienamine, valiolone, valiolamine, and 1-epi-valienol, were not incorporated and thus are not plausible intermediates in 1 biosynthesis. 2-epi-Valiolone (10b), which has the same stereochemistry as the presumed open-chain precursor, sedoheptulose 7-phosphate, was also not incorporated. However, its C-5 epimer (10a) was incorporated efficiently and specifically into the valienamine moiety of 1. Surprisingly, the dehydrated form of 2-epi-5-epi-valiolone, 2-epi-valienone, was not incorporated. This suggests that 2-epi-5-epi-valiolone must be converted directly into the pseudodisaccharide moiety of acarbose without the intervention of other free cyclitol intermediates. This may occur by linkage to the amino group of TDP-4-amino-4,6-dideoxyglucose to form. the imine, epimerization at C-2 to the correct stereochemistry, dehydration between C-5 and C-6 aided by enamine formation, and finally reduction to the amine. It is proposed that these reaction steps all take place on a single enzyme without free intermediates. Alternative mechanistic possibilities are also discussed.

  DOI：

  10.1021/ja991102w
• 作为产物：
  描述：

  2,3,4,6-tetra-O-benzyl-D-mannono-1,5-lactone 在 sodium tetrahydroborate 、 二甲基亚砜 、 三乙胺 、 三氟乙酸酐 、 lithium diisopropyl amide 作用下， 以 四氢呋喃 、 正庚烷 、 二乙二醇二甲醚 、 乙基苯 为溶剂， 反应 2.5h， 生成 (3S,4S,5S)-3,4,5,7-Tetrakis-benzyloxy-1,1-dichloro-heptane-2,6-dione
  参考文献：
  名称：

  Biosynthetic Studies on the α-Glucosidase Inhibitor Acarbose in Actinoplanes sp.:  2-epi-5-epi-Valiolone Is the Direct Precursor of the Valienamine Moiety

  摘要：

  The biosynthetic pathway leading to the mC(7)N cyclitol (valienamine) moiety of acarbose (1) in Actinoplanes sp. strain SN 223/29 has been studied using H-3-, H-2-, and C-13-labeled cyclitols. These precursors were synthesized from D-glucose or D-mannose as starting materials. The feeding experiments demonstrated that cyclitols having the same stereochemistry at C-2 as the valienamine moiety of acarbose; i.e., valienone, valienamine, valiolone, valiolamine, and 1-epi-valienol, were not incorporated and thus are not plausible intermediates in 1 biosynthesis. 2-epi-Valiolone (10b), which has the same stereochemistry as the presumed open-chain precursor, sedoheptulose 7-phosphate, was also not incorporated. However, its C-5 epimer (10a) was incorporated efficiently and specifically into the valienamine moiety of 1. Surprisingly, the dehydrated form of 2-epi-5-epi-valiolone, 2-epi-valienone, was not incorporated. This suggests that 2-epi-5-epi-valiolone must be converted directly into the pseudodisaccharide moiety of acarbose without the intervention of other free cyclitol intermediates. This may occur by linkage to the amino group of TDP-4-amino-4,6-dideoxyglucose to form. the imine, epimerization at C-2 to the correct stereochemistry, dehydration between C-5 and C-6 aided by enamine formation, and finally reduction to the amine. It is proposed that these reaction steps all take place on a single enzyme without free intermediates. Alternative mechanistic possibilities are also discussed.

  DOI：

  10.1021/ja991102w

文献信息

• Biosynthetic Studies on the α-Glucosidase Inhibitor Acarbose in <i>Actinoplanes</i> sp.:  2-<i>epi</i>-5-<i>epi</i>-Valiolone Is the Direct Precursor of the Valienamine Moiety
  作者：Taifo Mahmud、Ingo Tornus、Erin Egelkrout、Eckardt Wolf、Charmaine Uy、Heinz G. Floss、Sungsook Lee

  DOI：10.1021/ja991102w

  日期：1999.8.1

  The biosynthetic pathway leading to the mC(7)N cyclitol (valienamine) moiety of acarbose (1) in Actinoplanes sp. strain SN 223/29 has been studied using H-3-, H-2-, and C-13-labeled cyclitols. These precursors were synthesized from D-glucose or D-mannose as starting materials. The feeding experiments demonstrated that cyclitols having the same stereochemistry at C-2 as the valienamine moiety of acarbose; i.e., valienone, valienamine, valiolone, valiolamine, and 1-epi-valienol, were not incorporated and thus are not plausible intermediates in 1 biosynthesis. 2-epi-Valiolone (10b), which has the same stereochemistry as the presumed open-chain precursor, sedoheptulose 7-phosphate, was also not incorporated. However, its C-5 epimer (10a) was incorporated efficiently and specifically into the valienamine moiety of 1. Surprisingly, the dehydrated form of 2-epi-5-epi-valiolone, 2-epi-valienone, was not incorporated. This suggests that 2-epi-5-epi-valiolone must be converted directly into the pseudodisaccharide moiety of acarbose without the intervention of other free cyclitol intermediates. This may occur by linkage to the amino group of TDP-4-amino-4,6-dideoxyglucose to form. the imine, epimerization at C-2 to the correct stereochemistry, dehydration between C-5 and C-6 aided by enamine formation, and finally reduction to the amine. It is proposed that these reaction steps all take place on a single enzyme without free intermediates. Alternative mechanistic possibilities are also discussed.