benzyl 2-acetamido-2-deoxy-6-O-(dimethylphosphinyl)-α-D-mannopyranoside | 140659-99-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: benzyl 2-acetamido-2-deoxy-6-O-(dimethylphosphinyl)-α-D-mannopyranoside
• 英文别名: N-[(2S,3S,4R,5S,6R)-6-(dimethylphosphoryloxymethyl)-4,5-dihydroxy-2-phenylmethoxyoxan-3-yl]acetamide
• CAS: 140659-99-0
• 化学式: C₁₇H₂₆NO₇P
• 分子量: 387.37
• InChiKey: KWVACRUCUBSVTL-JJTUDDRGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.2
• 重原子数：
  26
• 可旋转键数：
  7
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.59
• 拓扑面积：
  114
• 氢给体数：
  3
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  benzyl 2-acetamido-2-deoxy-6-O-(dimethylphosphinyl)-α-D-mannopyranoside 在 palladium on activated charcoal DL-dithiothreitol 、 氢气 作用下， 以 乙醇 、 水 为溶剂， 反应 106.0h， 生成 9-O-(dimethylphosphinyl)-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 、 2,6-二甲基吡啶 、 三氟化硼乙醚 、 sodium methylate 作用下， 以 甲醇 、 硝基甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 23.0h， 生成 benzyl 2-acetamido-2-deoxy-6-O-(dimethylphosphinyl)-α-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

• 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
• US5461143A
  申请人：——

  公开号：US5461143A

  公开（公告）日：1995-10-24
• US5593887A
  申请人：——

  公开号：US5593887A

  公开（公告）日：1997-01-14
• US5759823A
  申请人：——

  公开号：US5759823A

  公开（公告）日：1998-06-02