2,6-anhydro-3,4,5,7-tetra-O-benzyl-1-deoxy-1-[(1-oxoethyl-2-acetoxy)amino]-D-glycero-D-ido-heptitol | 701981-05-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 2,6-anhydro-3,4,5,7-tetra-O-benzyl-1-deoxy-1-[(1-oxoethyl-2-acetoxy)amino]-D-glycero-D-ido-heptitol
• CAS: 701981-05-7
• 化学式: C₃₉H₄₃NO₈
• 分子量: 653.772
• InChiKey: OSPVUGTUHHLFAW-UVBAHNABSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.41
• 重原子数：
  48.0
• 可旋转键数：
  17.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  101.55
• 氢给体数：
  1.0
• 氢受体数：
  8.0

反应信息

• 作为反应物：
  描述：

  2,6-anhydro-3,4,5,7-tetra-O-benzyl-1-deoxy-1-[(1-oxoethyl-2-acetoxy)amino]-D-glycero-D-ido-heptitol 在 水 、 三乙胺 作用下， 以 甲醇 为溶剂， 反应 3.0h， 以96.7%的产率得到2,6-anhydro-3,4,5,7-tetra-O-benzyl-1-deoxy-1-[(1-oxoethyl-2-hydroxy)amino]-D-glycero-D-ido-heptitol
  参考文献：
  名称：

  Recognition Properties of Processing α‐Glucosidase I and α‐Glucosidase II

  摘要：

  All four possible monodeoxy derivatives of p-nitrophenyl alpha-D-glucopyranoside (PNP Glc) and 1-amino-2,6-anhydro-1-deOXY-D-glycero-D-ido-heptitol derivatives were prepared and used as substrates and inhibitors of rat liver processing alpha-glucosidases. alpha-Glucosidase II hydrolyzed the 2-deoxy derivative of PNP Glc (1); the hydrolysis of 1 was more rapid than that of PNP Glc. These results indicate that the presence of a C-2 hydroxyl group is not essential for the action of alpha-glucosidase II. In contrast, PNP Glc and all of the deoxy derivatives of PNP Glc 1-4 inhibited alpha-glucosidase I. These results indicate that alpha-glucosidase I does not necessarily need all of the hydroxyl groups of the glycon moiety for binding to the enzyme. 2,6-Anhydro-1-benzamide-D-glycero-D-ido-heptitol (11), with a terminal phenyl group, inhibited a-glucosidase I and a-glucosidase II. Both alpha-glucosidase I and II showed the same aglycon specificities. When probes 5-12 were assayed for their ability to inhibit processing by a-glucosidases at the cellular level, no effects on glycoprotein processing were observed.

  DOI：

  10.1081/car-120030022
• 作为产物：
  描述：

  2,3,4,6-tetra-O-benzyl-α-D-glucopyranosyl cyanide 在 lithium aluminium tetrahydride 、 二苯基膦叠氮化物 、 三乙胺 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 9.0h， 生成 2,6-anhydro-3,4,5,7-tetra-O-benzyl-1-deoxy-1-[(1-oxoethyl-2-acetoxy)amino]-D-glycero-D-ido-heptitol
  参考文献：
  名称：

  Recognition Properties of Processing α‐Glucosidase I and α‐Glucosidase II

  摘要：

  All four possible monodeoxy derivatives of p-nitrophenyl alpha-D-glucopyranoside (PNP Glc) and 1-amino-2,6-anhydro-1-deOXY-D-glycero-D-ido-heptitol derivatives were prepared and used as substrates and inhibitors of rat liver processing alpha-glucosidases. alpha-Glucosidase II hydrolyzed the 2-deoxy derivative of PNP Glc (1); the hydrolysis of 1 was more rapid than that of PNP Glc. These results indicate that the presence of a C-2 hydroxyl group is not essential for the action of alpha-glucosidase II. In contrast, PNP Glc and all of the deoxy derivatives of PNP Glc 1-4 inhibited alpha-glucosidase I. These results indicate that alpha-glucosidase I does not necessarily need all of the hydroxyl groups of the glycon moiety for binding to the enzyme. 2,6-Anhydro-1-benzamide-D-glycero-D-ido-heptitol (11), with a terminal phenyl group, inhibited a-glucosidase I and a-glucosidase II. Both alpha-glucosidase I and II showed the same aglycon specificities. When probes 5-12 were assayed for their ability to inhibit processing by a-glucosidases at the cellular level, no effects on glycoprotein processing were observed.

  DOI：

  10.1081/car-120030022