2-acetamido-6-azido-2,6-dideoxy-α-D-mannopyranoside | 140660-05-5

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 2-acetamido-6-azido-2,6-dideoxy-α-D-mannopyranoside
• 英文别名: 2-acetamido-6-azido-2,6-dideoxy-α-D-mannopyranose；N-[(2S,3S,4R,5S,6R)-6-(azidomethyl)-2,4,5-trihydroxyoxan-3-yl]acetamide
• CAS: 140660-05-5
• 化学式: C₈H₁₄N₄O₅
• 分子量: 246.223
• InChiKey: JBCJECOTKGFRTM-UOLFYFMNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.6
• 重原子数：
  17
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  113
• 氢给体数：
  4
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  sodium pyruvate 、 2-acetamido-6-azido-2,6-dideoxy-α-D-mannopyranoside 在 DL-dithiothreitol 作用下， 反应 14.0h， 以84%的产率得到9-azido-9-deoxy-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 、 sodium azide 、 三氟化硼乙醚 、 sodium methylate 、 sodium acetate 、 溶剂黄146 、 sodium iodide 、 palladium dichloride 作用下， 以 甲醇 、 硝基甲烷 、 二氯甲烷 、 N,N-二甲基甲酰胺 、 丁酮 为溶剂， 反应 49.58h， 生成 2-acetamido-6-azido-2,6-dideoxy-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

• A FRET Probe for Cell-Based Imaging of Ganglioside-Processing Enzyme Activity and High-Throughput Screening
  作者：Guang-Yu Yang、Caishun Li、Michael Fischer、Christopher W. Cairo、Yan Feng、Stephen G. Withers

  DOI：10.1002/anie.201411747

  日期：2015.4.27

  in living cells. This is the first substrate that enables the ratiometric fluorogenic assay of sphingolipid ceramide N‐deacylase and endoglycoceramidase and can detect and localize neuraminidase activity in living cells. It is therefore a valuable tool for building a better understanding of membrane‐confined enzymology. It also enables the robust and reliable assay of ganglioside‐degrading enzymes in

  神经节苷脂是细胞膜中重要的信号分子，并由几种酶处理。这些酶的缺乏会导致人类溶酶体贮积病。建立对糖鞘脂分解代谢途径的了解需要分析这些酶活性的方法。通过化学方法合成了GM3衍生的FRET探针，用于检测和定量细胞裂解液和活细胞中各种神经节苷脂降解酶。这是第一个能够对鞘脂神经酰胺N-脱酰基酶和糖苷内酰胺酶进行荧光定量测定并能检测和定位活细胞中神经氨酸酶活性的底物。因此，它是建立对膜限制酶学的更好理解的有价值的工具。
• 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