β-D-Man-F | 210281-95-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: β-D-Man-F
• 英文别名: β-D-mannopyranosyl fluoride；β-mannosyl fluoride；beta-Mannosyl fluoride；(2S,3S,4S,5S,6R)-2-fluoro-6-(hydroxymethyl)oxane-3,4,5-triol
• CAS: 210281-95-1
• 化学式: C₆H₁₁FO₅
• 分子量: 182.149
• InChiKey: ATMYEINZLWEOQU-RWOPYEJCSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.6
• 重原子数：
  12
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  90.2
• 氢给体数：
  4
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  β-D-Man-F 在 mutant malA D₃₂₀G from Sulfolobus solfataricus 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 192.0h， 生成
  参考文献：
  名称：

  从广泛的糖苷酶支架创建α-甘露糖合成酶

  摘要：

  α-甘露糖苷变得容易：GH31 α-葡萄糖苷酶家族的突变对供体底物的 2-OH 位置的改变显示出可塑性，创造了一种有效的 α-甘露糖苷合成生物催化剂。使用显示低（不需要的）寡聚化活性的 α-甘露糖合酶，将一种简单的氟化物供体试剂用于合成一系列单-α-甘露糖基化偶联物。

  DOI：

  10.1002/anie.201201081
• 作为产物：
  描述：

  2,5-dinitrophenyl β-D-mannopyranoside 在 potassium fluoride 、 Cellulomonas fimi β-mannoside (Man2A E429A) 作用下， 以 水 为溶剂， 反应 0.33h， 生成 β-D-Man-F
  参考文献：
  名称：

  碳氟键的酶促合成。

  摘要：

  DOI：

  10.1021/ja005855q

文献信息

• Enzymatic synthesis of disaccharides using Agrobacterium sp. β-glucosidase
  作者：Heiko Prade、Lloyd F. Mackenzie、Stephen G. Withers

  DOI：10.1016/s0008-6215(97)10040-4

  日期：1997.12

  yields up to 65%, has been achieved by utilizing the transglycosylation activity of Agrobacterium sp. β-glucosidase (EC 3.2.1.21). The regioselectivity of the glycosylation reaction was investigated using p -nitrophenyl β- d -galactopyranoside, β- d -mannopyranosyl fluoride and d -glucal as glycosyl donors and a series of phenyl 1-thio-, benzyl 1-thio-, and benzyl β- d -glycopyranosides as glycosyl acceptors

  摘要利用土壤杆菌属（Agrobacterium sp。）的转糖基化活性已经实现了几种寡糖的合成，收率高达65％。β-葡萄糖苷酶（EC 3.2.1.21）。使用对硝基苯基β-d-吡喃半乳糖苷，β-d-甘露吡喃糖基氟化物和d-葡萄糖醛作为糖基供体以及一系列苯基1-硫代，苄基1-硫代和苄基β研究了糖基化反应的区域选择性-d-糖吡喃糖苷作为糖基受体。确定分离出的产物对于所有糖基受体均含有β-（1→3）和/或β-（1→4）糖苷键的混合物，但β-d-半乳糖构型受体除外，其中β-的混合物为-观察到（1→3）和β-（1→6）键。
• Simultaneous detection of different glycosidase activities by 19F NMR spectroscopy
  作者：Martin Albert、Werner Repetschnigg、Jörg Ortner、Joseph Gomes、Bernhard J. Paul、Carina Illaszewicz、Hansjörg Weber、Walter Steiner、Karl Dax

  DOI：10.1016/s0008-6215(00)00060-4

  日期：2000.8

  A fast method for the simultaneous detection of different glycosidolytic activities in commercially available enzyme preparations and crude culture filtrates was found in using, as substrate, a mixture of different glycosyl fluorides and F-19 NMR spectroscopy as a screening technique. Accompanying studies regarding the hydrolytic stability of these fluorides in various buffer systems, as well as conditions of their long-term storage, were carried out. A simple procedure for the preparation of beta-D-mannopyranosyl fluoride in gram quantities is given. (C) 2000 Elsevier Science Ltd. All rights reserved.
• Transglycosylation reactions with a crude culture filtrate from Thermoascusaurantiacus
  作者：Jörg Ortner、Martin Albert、Katherine Terler、Walter Steiner、Karl Dax

  DOI：10.1016/s0008-6215(00)00061-6

  日期：2000.8

  Some characteristics of regioselectivity and acceptor tolerance in transglycosylation reactions, catalysed by a crude culture filtrate from Thermoascus aurantiacus, were examined by employing methanol and monosaccharides as accepters. When beta-D-mannopyranosyl fluoride was employed as the donor, the anomeric configuration of the newly formed bond was found to depend on the structure of the acceptor used. (C) 2000 Elsevier Science Ltd. All rights reserved.
• Enzymatic Synthesis of Carbon−Fluorine Bonds
  作者：David L. Zechel、Stephen P. Reid、Oyekanmi Nashiru、Christoph Mayer、Dominik Stoll、David L. Jakeman、R. Antony J. Warren、Stephen G. Withers

  DOI：10.1021/ja005855q

  日期：2001.5.1
• Creation of an α-Mannosynthase from a Broad Glycosidase Scaffold
  作者：Keisuke Yamamoto、Benjamin G. Davis

  DOI：10.1002/anie.201201081

  日期：2012.7.23

  α‐Mannosides made easy: Mutation of a family‐GH31 α‐glucosidase that displays plasticity to alterations at the 2‐OH position of donor substrates created an efficient α‐mannoside‐synthesizing biocatalyst. A simple fluoride donor reagent was used for the synthesis of a range of mono‐α‐mannosylated conjugates using the α‐mannosynthase displaying low (unwanted) oligomerization activity.

  α-甘露糖苷变得容易：GH31 α-葡萄糖苷酶家族的突变对供体底物的 2-OH 位置的改变显示出可塑性，创造了一种有效的 α-甘露糖苷合成生物催化剂。使用显示低（不需要的）寡聚化活性的 α-甘露糖合酶，将一种简单的氟化物供体试剂用于合成一系列单-α-甘露糖基化偶联物。