allyl 2-acetamido-2,6-dideoxy-6-fluoro-a-D-mannopyranoside | 146912-88-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: allyl 2-acetamido-2,6-dideoxy-6-fluoro-a-D-mannopyranoside
• 英文别名: allyl 2-acetamido-2,6-dideoxy-6-fluoro-alpha-D-mannopyranoside；N-[(2S,3S,4R,5S,6S)-6-(fluoromethyl)-4,5-dihydroxy-2-prop-2-enoxyoxan-3-yl]acetamide
• CAS: 146912-88-1
• 化学式: C₁₁H₁₈FNO₅
• 分子量: 263.266
• InChiKey: BAVVRKJTNUKFIN-QGKZMRNZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.9
• 重原子数：
  18
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.73
• 拓扑面积：
  88
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  allyl 2-acetamido-2,6-dideoxy-6-fluoro-a-D-mannopyranoside 在 DL-dithiothreitol 、 sodium acetate 、 palladium diacetate 、 溶剂黄146 作用下， 反应 210.0h， 生成 9-deoxy-9-fluoro-N-acetylneuraminic acid
  参考文献：
  名称：

  Overproduction of CMP-sialic acid synthetase for organic synthesis

  摘要：

  The gene coding for Escherichia coli CMP-sialic acid synthetase (E.C. 2.7.7.43) was cloned and overexpressed in E. coli through a primer-directed polymerase chain reaction. Two plasmids were constructed to produce the native enzyme and a modified enzyme fused with a decapeptide at the C-terminus. The decapeptide tag was used for detection of the enzyme production. Both enzymes produced from E. coli were isolated and purified with an Orange A dye resin and FPLC. Their properties were compared with respect to their kinetic parameters, stability, pH profiles, and substrate specificities. Both enzymes have similar k(cat) and K(m) for NeuAc and CTP but different pH profiles. Contrary to the native enzyme, the modified enzyme is more active at higher pH. Studies on specificity indicate that both enzymes have a high specific activity for C-9 modified NeuAc derivatives at neutral pH. Some C-5 modified (hydroxy, deoxy, and deoxyfluoro) NeuAc derivatives are not acceptable as substrates. The modified enzyme has been used in the synthesis of CMP-NeuAc from ManNAc and CMP and sialyl N-acetyllactosamine (Neu-alpha-2,6Gal-beta-1,4GlcNAc) with in situ generation of NeuAc and regeneration of CMP-NeuAc. The 6-O-acyl derivatives of ManNAc were prepared via transesterification in anhydrous dimethylformamide by using an engineered stable subtilisin variant as a catalyst, and the products were used as substrates in sialic acid aldolase-catalyzed synthesis of 9-O-acyl-NeuAc derivatives.

  DOI：

  10.1021/ja00036a044
• 作为产物：
  描述：

  N-acetyl-D-mannosamine 在 吡啶 、 二乙胺基三氟化硫 、 三氟化硼乙醚 、 sodium methylate 、 溶剂黄146 作用下， 以 甲醇 、 硝基甲烷 、 二乙二醇二甲醚 为溶剂， 反应 119.83h， 生成 allyl 2-acetamido-2,6-dideoxy-6-fluoro-a-D-mannopyranoside
  参考文献：
  名称：

  Overproduction of CMP-sialic acid synthetase for organic synthesis

  摘要：

  The gene coding for Escherichia coli CMP-sialic acid synthetase (E.C. 2.7.7.43) was cloned and overexpressed in E. coli through a primer-directed polymerase chain reaction. Two plasmids were constructed to produce the native enzyme and a modified enzyme fused with a decapeptide at the C-terminus. The decapeptide tag was used for detection of the enzyme production. Both enzymes produced from E. coli were isolated and purified with an Orange A dye resin and FPLC. Their properties were compared with respect to their kinetic parameters, stability, pH profiles, and substrate specificities. Both enzymes have similar k(cat) and K(m) for NeuAc and CTP but different pH profiles. Contrary to the native enzyme, the modified enzyme is more active at higher pH. Studies on specificity indicate that both enzymes have a high specific activity for C-9 modified NeuAc derivatives at neutral pH. Some C-5 modified (hydroxy, deoxy, and deoxyfluoro) NeuAc derivatives are not acceptable as substrates. The modified enzyme has been used in the synthesis of CMP-NeuAc from ManNAc and CMP and sialyl N-acetyllactosamine (Neu-alpha-2,6Gal-beta-1,4GlcNAc) with in situ generation of NeuAc and regeneration of CMP-NeuAc. The 6-O-acyl derivatives of ManNAc were prepared via transesterification in anhydrous dimethylformamide by using an engineered stable subtilisin variant as a catalyst, and the products were used as substrates in sialic acid aldolase-catalyzed synthesis of 9-O-acyl-NeuAc derivatives.

  DOI：

  10.1021/ja00036a044

文献信息

• Oligosaccharide enzyme substrates and inhibitors: methods and
  申请人：The Scripps Research Institute

  公开号：US05593887A1

  公开（公告）日：1997-01-14

  Oligosacaharide compounds that are substrates and inhibitors of glycosyltransferase and glycosidase enzymes and compositions containing such compounds are disclosed. A method of glycosylation is also disclosed. An E. coli transformed with phagemid CMPSIL-1, which phagemid comprises a gene for a modified CMP-sialic acid synthetase enzyme, which transformed E. coli has the ATCC accession No. 68531 is also provided.

  本发明公开了一种寡糖化合物，它们是糖基转移酶和糖苷酶酶的底物和抑制剂，以及含有这种化合物的组合物。还公开了一种糖基化方法。本发明还提供了一种转化有噬菌体质粒CMPSIL-1的大肠杆菌，该噬菌体质粒包括一种修饰的CMP-唾液酸合成酶酶基因，所述转化的大肠杆菌的ATCC存储编号为68531。
• Ogligosaccharide enzyme substrates and inhibitors: methods and
  申请人：Scripps Research Institute

  公开号：US05759823A1

  公开（公告）日：1998-06-02

  Oligosaccharide compounds that are substrates and inhibitors of glycosyltransferase and glycosidase enzymes and compositions containing such compounds are disclosed. A method of glycosylation is also disclosed. An E. coli transformed with phagemid CMPSIL-1, which phagemid comprises a gene for a modified CMP-sialic acid synthetase enzyme, which transformed E. coli has the ATCC accession No. 68531 is also provided.

  本发明揭示了作为糖基转移酶和糖苷酶酶底物和抑制剂的寡糖化合物以及含有这些化合物的组合物。还揭示了一种糖基化方法。提供了一种转化有噬菌体质粒CMPSIL-1的大肠杆菌，该噬菌体质粒包含一个修饰的CMP-唾液酸合成酶酶基因，该转化的大肠杆菌的ATCC编号为68531。
• US06168934A
  申请人：——

  公开号：——

  公开（公告）日：——
• EP0576592A4
  申请人：——

  公开号：EP0576592A4

  公开（公告）日：1996-01-24
• OLIGOSACCHARIDE ENZYME SUBSTRATES AND INHIBITORS: METHODS AND COMPOSITIONS
  申请人：THE SCRIPPS RESEARCH INSTITUTE

  公开号：EP0576592B1

  公开（公告）日：2000-05-31