O-(3,6-anhydro-α-D-glucopyranosyl)-(1->4)-tris4)>-D-glucopyranose

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: O-(3,6-anhydro-α-D-glucopyranosyl)-(1->4)-tris4)>-D-glucopyranose
• 英文别名: O-(3,6-anhydro-α-D-glucopyranosyl)-(1->4)-tris[O-α-D-glucopyranosyl-(1->4)]-D-glucopyranose；(3R,4R,5S,6R)-5-[(2R,3R,4R,5S,6R)-5-[(2R,3R,4R,5S,6R)-5-[(2R,3R,4R,5S,6R)-5-[[(1R,3R,4R,5S,8R)-4,8-dihydroxy-2,6-dioxabicyclo[3.2.1]octan-3-yl]oxy]-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-6-(hydroxymethyl)oxane-2,3,4-triol
• 化学式: C₃₀H₅₀O₂₅
• 分子量: 810.712
• InChiKey: AVHAUORGNHVXFP-VEZIRVFZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -10.7
• 重原子数：
  55
• 可旋转键数：
  12
• 环数：
  6.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  396
• 氢给体数：
  15
• 氢受体数：
  25

反应信息

• 作为反应物：
  描述：

  乙酸酐 、 O-(3,6-anhydro-α-D-glucopyranosyl)-(1->4)-tris4)>-D-glucopyranose 在 吡啶 作用下， 反应 48.0h， 生成
  参考文献：
  名称：

  Syntheses of subtractively modified 2-chloro-4-nitrophenyl β-maltopentaosides and their application to the differential assay of human alpha-amylases

  摘要：

  Three novel maltopentaosides, 2-chloro-4-nitrophenyl O-(6-deoxy-alpha-D-xylo-hex-5-enopyranosyl)-(1 --> 4)-tris[O-alpha-D-glucopyranosyl-(1 --> 4)]-beta-D-glucopyranoside (3), 2-chloro-4-nitrophenyl O-(6-deoxy-alpha-D-glucopyranosyl)-(1 --> 4)-tris[O-alpha-D-glucopyranosyl-(1 --> 4)]-beta-D-glucopyranoside (10), and 2-chloro-4-nitrophenyl O-(3,6-anhydro-alpha-D-glucopyranosyl)-(1 --> 4)-tris[O-alpha-D-glucopyranosyl-(1 --> 4)]-beta-D-glucopyranoside (26) were synthesized by chemical and enzymatic reactions. Two human alpha-amylases, salivary alpha-amylase (HSA) and pancreatic alpha-amylase (HPA), hydrolyzed 3 and 10 with the same specificity, almost entirely at a single D-glucosidic linkage, but had no hydrolytic acitivity for 26. Compound 3 was hydrolyzed by each of these amylases at an approximately equal rate, while 10 was hydrolyzed by HSA 4-fold faster than by HPA. Taking advantage of the difference in the hydrolytic rate of 10, we developed a new method for the differential assay of these two human alpha-amylases.

  DOI：

  10.1016/0008-6215(93)87013-i
• 作为产物：
  描述：

  Mono-3^A,6^A-anhydrocyclomaltoheptaose 生成 D-葡萄糖 、 O-(3,6-anhydro-α-D-glucopyranosyl)-(1->4)-bis4)>-D-glucopyranose 、 O-(3,6-anhydro-α-D-glucopyranosyl)-(1->4)-tris4)>-D-glucopyranose 、 O-(3,6-anhydro-α-D-glucopyranosyl)-(1->4)-tetrakis4)>-D-glucopyranose
  参考文献：
  名称：

  Syntheses of subtractively modified 2-chloro-4-nitrophenyl β-maltopentaosides and their application to the differential assay of human alpha-amylases

  摘要：

  Three novel maltopentaosides, 2-chloro-4-nitrophenyl O-(6-deoxy-alpha-D-xylo-hex-5-enopyranosyl)-(1 --> 4)-tris[O-alpha-D-glucopyranosyl-(1 --> 4)]-beta-D-glucopyranoside (3), 2-chloro-4-nitrophenyl O-(6-deoxy-alpha-D-glucopyranosyl)-(1 --> 4)-tris[O-alpha-D-glucopyranosyl-(1 --> 4)]-beta-D-glucopyranoside (10), and 2-chloro-4-nitrophenyl O-(3,6-anhydro-alpha-D-glucopyranosyl)-(1 --> 4)-tris[O-alpha-D-glucopyranosyl-(1 --> 4)]-beta-D-glucopyranoside (26) were synthesized by chemical and enzymatic reactions. Two human alpha-amylases, salivary alpha-amylase (HSA) and pancreatic alpha-amylase (HPA), hydrolyzed 3 and 10 with the same specificity, almost entirely at a single D-glucosidic linkage, but had no hydrolytic acitivity for 26. Compound 3 was hydrolyzed by each of these amylases at an approximately equal rate, while 10 was hydrolyzed by HSA 4-fold faster than by HPA. Taking advantage of the difference in the hydrolytic rate of 10, we developed a new method for the differential assay of these two human alpha-amylases.

  DOI：

  10.1016/0008-6215(93)87013-i

文献信息

• Syntheses of subtractively modified 2-chloro-4-nitrophenyl β-maltopentaosides and their application to the differential assay of human alpha-amylases
  作者：Shoichi Tokutake、Tetsuya Oguma、Kouichirou Tobe、Kazuo Kotani、Kazunori Saito、Nobuyuki Yamaji

  DOI：10.1016/0008-6215(93)87013-i

  日期：1993.1

  Three novel maltopentaosides, 2-chloro-4-nitrophenyl O-(6-deoxy-alpha-D-xylo-hex-5-enopyranosyl)-(1 --> 4)-tris[O-alpha-D-glucopyranosyl-(1 --> 4)]-beta-D-glucopyranoside (3), 2-chloro-4-nitrophenyl O-(6-deoxy-alpha-D-glucopyranosyl)-(1 --> 4)-tris[O-alpha-D-glucopyranosyl-(1 --> 4)]-beta-D-glucopyranoside (10), and 2-chloro-4-nitrophenyl O-(3,6-anhydro-alpha-D-glucopyranosyl)-(1 --> 4)-tris[O-alpha-D-glucopyranosyl-(1 --> 4)]-beta-D-glucopyranoside (26) were synthesized by chemical and enzymatic reactions. Two human alpha-amylases, salivary alpha-amylase (HSA) and pancreatic alpha-amylase (HPA), hydrolyzed 3 and 10 with the same specificity, almost entirely at a single D-glucosidic linkage, but had no hydrolytic acitivity for 26. Compound 3 was hydrolyzed by each of these amylases at an approximately equal rate, while 10 was hydrolyzed by HSA 4-fold faster than by HPA. Taking advantage of the difference in the hydrolytic rate of 10, we developed a new method for the differential assay of these two human alpha-amylases.