α-isomaltosyl-(1->4)-maltopentaose

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: α-isomaltosyl-(1->4)-maltopentaose
• 英文别名: Glc(a1-6)Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc；(2S,3R,4S,5S,6R)-2-[[(2R,3S,4S,5R,6R)-6-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2R,3S,4R,5R)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-3,4,5-trihydroxyoxan-2-yl]methoxy]-6-(hydroxymethyl)oxane-3,4,5-triol
• 化学式: C₄₂H₇₂O₃₆
• 分子量: 1153.01
• InChiKey: JJWWZMRAGRVCFZ-MBQDTMIWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -15.5
• 重原子数：
  78
• 可旋转键数：
  19
• 环数：
  7.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  585
• 氢给体数：
  23
• 氢受体数：
  36

反应信息

• 作为反应物：
  描述：

  α-isomaltosyl-(1->4)-maltopentaose 在 3-吗啉丙磺酸 、 cycloalternan-forming enzyme from Bacillus sp. NRRL B₂₁₁₉₅ 作用下， 生成 cyclo-{->6)-α-D-Glcp-(1->3)-α-D-Glcp-(1->6)-α-D-Glcp-(1->3)-α-D-Glcp-(1->}
  参考文献：
  名称：

  A synergistic reaction mechanism of a cycloalternan-forming enzyme and a d-glucosyltransferase for the production of cycloalternan in Bacillus sp. NRRL B-21195

  摘要：

  Cycloalternan-forming enzyme (CAFE) was first described as the enzyme that produced cycloalternan from alternan. In this study, we found that a partially purified preparation of CAFE containing two proteins catalyzed the synthesis of cycloalternan from maltooligosaccharides, whereas the purified CAFE alone was unable to do so. In addition to the 117 kDa CAFE itself, the mixture also contained a 140 kDa protein. The latter was found to be a disproportionating enzyme (DE) that catalyzes transfer of a D-glucopyranosyl residue from the non-reducing end of one maltooligosaccharide to the non-reducing end of another, forming an isomaltosyl residue at the non-reducing end. CAFE then transfers the isomaltosyl residue to the non-reducing end of another isomaltosyl maltooligosaccharide, to form an alpha-isomaltosyl-(1-->3)-alpha-isomaltosyl-(1-->4)-maltooligosaccharide, and subsequently catalyzes a cyclization to produce cycloalternan. Thus, DE and CAFE act synergistically to produce cycloalternan directly from maltodextrin or starch. (C) 2003 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/s0008-6215(03)00375-6
• 作为产物：
  描述：

  D-maltohexaose 在 3-吗啉丙磺酸 、 disproportionating enzyme from Bacillus sp. NRRL B-21195 作用下， 反应 40.0h， 生成 α-isomaltosyl-(1->4)-maltopentaose
  参考文献：
  名称：

  A synergistic reaction mechanism of a cycloalternan-forming enzyme and a d-glucosyltransferase for the production of cycloalternan in Bacillus sp. NRRL B-21195

  摘要：

  Cycloalternan-forming enzyme (CAFE) was first described as the enzyme that produced cycloalternan from alternan. In this study, we found that a partially purified preparation of CAFE containing two proteins catalyzed the synthesis of cycloalternan from maltooligosaccharides, whereas the purified CAFE alone was unable to do so. In addition to the 117 kDa CAFE itself, the mixture also contained a 140 kDa protein. The latter was found to be a disproportionating enzyme (DE) that catalyzes transfer of a D-glucopyranosyl residue from the non-reducing end of one maltooligosaccharide to the non-reducing end of another, forming an isomaltosyl residue at the non-reducing end. CAFE then transfers the isomaltosyl residue to the non-reducing end of another isomaltosyl maltooligosaccharide, to form an alpha-isomaltosyl-(1-->3)-alpha-isomaltosyl-(1-->4)-maltooligosaccharide, and subsequently catalyzes a cyclization to produce cycloalternan. Thus, DE and CAFE act synergistically to produce cycloalternan directly from maltodextrin or starch. (C) 2003 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/s0008-6215(03)00375-6

文献信息

• A synergistic reaction mechanism of a cycloalternan-forming enzyme and a d-glucosyltransferase for the production of cycloalternan in Bacillus sp. NRRL B-21195
  作者：Yeon-Kye Kim、Motomitsu Kitaoka、Kiyoshi Hayashi、Cheorl-Ho Kim、Gregory L. Côté

  DOI：10.1016/s0008-6215(03)00375-6

  日期：2003.10

  Cycloalternan-forming enzyme (CAFE) was first described as the enzyme that produced cycloalternan from alternan. In this study, we found that a partially purified preparation of CAFE containing two proteins catalyzed the synthesis of cycloalternan from maltooligosaccharides, whereas the purified CAFE alone was unable to do so. In addition to the 117 kDa CAFE itself, the mixture also contained a 140 kDa protein. The latter was found to be a disproportionating enzyme (DE) that catalyzes transfer of a D-glucopyranosyl residue from the non-reducing end of one maltooligosaccharide to the non-reducing end of another, forming an isomaltosyl residue at the non-reducing end. CAFE then transfers the isomaltosyl residue to the non-reducing end of another isomaltosyl maltooligosaccharide, to form an alpha-isomaltosyl-(1-->3)-alpha-isomaltosyl-(1-->4)-maltooligosaccharide, and subsequently catalyzes a cyclization to produce cycloalternan. Thus, DE and CAFE act synergistically to produce cycloalternan directly from maltodextrin or starch. (C) 2003 Elsevier Ltd. All rights reserved.