N-[(2S,3S,4R,5S,6R)-4,5-dihydroxy-2-prop-2-enoxy-6-(trityloxymethyl)oxan-3-yl]acetamide | 63064-55-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: N-[(2S,3S,4R,5S,6R)-4,5-dihydroxy-2-prop-2-enoxy-6-(trityloxymethyl)oxan-3-yl]acetamide
• CAS: 63064-55-1；65947-35-5
• 化学式: C₃₀H₃₃NO₆
• 分子量: 503.595
• InChiKey: VBZIPFBJVYNANW-FOECPVOOSA-N

物化性质

• 沸点：
  702.0±60.0 °C(Predicted)
• 密度：
  1.25±0.1 g/cm3(Temp: 20 °C; Press: 760 Torr)(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  37
• 可旋转键数：
  10
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  97.2
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  N-[(2S,3S,4R,5S,6R)-4,5-dihydroxy-2-prop-2-enoxy-6-(trityloxymethyl)oxan-3-yl]acetamide 在 DL-dithiothreitol 、 二乙胺基三氟化硫 、 sodium methylate 、 sodium acetate 、 palladium diacetate 、 溶剂黄146 作用下， 以 甲醇 、 二乙二醇二甲醚 为溶剂， 反应 305.33h， 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 、 三氟化硼乙醚 、 sodium methylate 作用下， 以 甲醇 、 硝基甲烷 为溶剂， 反应 24.5h， 生成 N-[(2S,3S,4R,5S,6R)-4,5-dihydroxy-2-prop-2-enoxy-6-(trityloxymethyl)oxan-3-yl]acetamide
  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

• 2-acylamino-2-deoxy-glucono-1,5-lactones, a method for the production thereof, compositions containing them, and uses thereof
  申请人：——

  公开号：US20020028954A1

  公开（公告）日：2002-03-07

  The invention concerns compounds of formula (I) wherein: A represents R 1 or (O)R 1 where R 1 represents an alkyl group comprising 1 to 30 carbon atoms, linear or branched, saturated or unsaturated, capable of being partly or totally substituted by Hal where Hal represents —Cl, —Br, or —F, and of being interrupted by one or several units selected among —O—, —S—, —C(O)—, —NR 3 C(O)—, —Ph(R 4 ) n and —CH 2 —CH 2 —O) n —, wherein R 3 represents or —CH 2 ) n″ —CH where n″=0 to 17; R 4 represents, —CH 3 , —CH 2 H 5 , —C 3 H 7 and n=0 to 4 and n′=1, 2 or 3, or R 1 represents a cyclanic radical with diterpene or triterpene root; and R 2 represents a C 1 -C 11 linear or branched alkyl group. The invention also concerns a method for obtaining said compounds, compositions containing them and their use as surfactant, and in enzymatic processes using a chitinase, in particular N-acetylglucosaminidase.

  该发明涉及以下式(I)的化合物：其中：A代表R1或（O）R1，其中R1代表由1至30个碳原子组成的烷基基团，直链或支链，饱和或不饱和，可以部分或完全被Hal取代，其中Hal代表-Cl，-Br或-F，并且可以被选自-O-，-S-，-C(O)-，-NR3C(O)-，-Ph(R4)n和-CH2-CH2-O)n-的一个或多个单位中断，其中R3代表或-CH2)n″-CH2，其中n″=0至17；R4代表-CH3，-CH2H5，-C3H7和n=0至4，n′=1，2或3，或者R1代表带有二萜或三萜基团的环烷基基团；R2代表C1-C11直链或支链烷基基团。该发明还涉及一种获得所述化合物的方法，含有它们的组合物以及它们作为表面活性剂的用途，以及在使用壳聚糖酶，特别是N-乙酰葡萄糖氨基酶的酶促过程中的用途。
• US6624190B2
  申请人：——

  公开号：US6624190B2

  公开（公告）日：2003-09-23
• Overproduction of CMP-sialic acid synthetase for organic synthesis
  作者：Jennifer Lin Chun Liu、Gwo Jenn Shen、Yoshitaka Ichikawa、James F. Rutan、Gerardo Zapata、Willie F. Vann、Chi Huey Wong

  DOI：10.1021/ja00036a044

  日期：1992.5

  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.