| 1338320-74-3

• 分子结构分类: 有机化合物 - 有机氧化合物
• CAS: 1338320-74-3
• 化学式: C₇₂H₁₂₂N₈O₄₇S
• 分子量: 1883.85
• InChiKey: AMVUQDWAYCIUTO-QINGVCARSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -18.91
• 重原子数：
  128.0
• 可旋转键数：
  34.0
• 环数：
  9.0
• sp3杂化的碳原子比例：
  0.9
• 拓扑面积：
  830.09
• 氢给体数：
  31.0
• 氢受体数：
  48.0

反应信息

• 作为反应物：
  描述：

  α-galactosyl fluoride 、 在 galactosynthase His₆BgaC/Glu₂₃₃Gly from Bacillus circulans 、 potassium chloride 、 sodium hydroxide 作用下， 以 aq. phosphate buffer 为溶剂， 生成
  参考文献：
  名称：

  糖基转移酶和糖合酶在顺序反应和一锅反应中的组合，用于合成1型和2型N-乙酰乙酰氨基低聚物

  摘要：

  N-乙酰基乳糖胺（LacNAc）1型和2型以及poly-LacNAc的二糖单元参与许多生物识别事件。我们通过两种重组糖基转移酶β1,3的组合报告了1型（3Galβ1-3GlcNAcβ1-; Gal = d-半乳糖，GlcNAc = N-乙酰基d-葡糖胺）和2型（3Galβ1-4GlcNAcβ1-4）的LacNAc寡聚体的模块化设计。- ñ从-acetylglucosaminyltransferase幽门螺杆菌和人类β1,4半乳糖转移酶1，用galactosynthase他6 BgaC / Glu233Gly从环状芽孢杆菌。他的6 BgaC / Glu233Gly和β1,3- N的组合顺序或单罐模式下的‐乙酰氨基葡萄糖氨基转移酶可产生最多四个LacNAc单元的LacNAc 1型寡聚体。此外，顺序使用所有这三种酶可以访问各种neo-LacNAc低聚物。我们介绍了由1型和2型交替单元和1型终止的LacNAc

  DOI：

  10.1002/cctc.201500645
• 作为产物：
  描述：

  、 uridine 5'-diphospho-N-acetylglucosamine 在 β1,3-N-acetylglucosaminyltransferase from Helicobacter pylori 、 human β-1,4-galactosyltransferase-1 、 potassium chloride 、 magnesium chloride 、 1,4-二巯基-2,3-丁二醇 作用下， 以 水 为溶剂， 生成 、 、
  参考文献：
  名称：

  Combinatorial One-Pot Synthesis of Poly-N-acetyllactosamine Oligosaccharides with Leloir-Glycosyltransferases

  摘要：

  AbstractPoly‐N‐acetyllactosamine (Poly‐LacNAc, [3Galβ1,4GlcNAcβ1]n) glycans play an essential role in carbohydrate‐protein interactions. The synthesis of poly‐LacNAc, both chemical and enzymatic, is typically characterized by high losses of product during sequential synthesis, due to deprotection and/or purification steps. In this work we present a one‐pot synthesis of poly‐LacNAc oligosaccharides by combining recombinant glycosyltransferases. By fractionation of the poly‐LacNAc glycan mixture we were able to isolate glycans with up to six N‐acetyllactosamine (LacNAc) units. Activity measurements of the involved recombinant β1,4‐galactosyltransferase‐1 (β4GalT‐1) and β1,3‐N‐acetylglucosaminyltransferase (β3GlcNAcT) with isolated glycan substrates of up to eight sugar units revealed a preference of β3GlcNAcT for the tetrasaccharide and no preference of β4GalT‐1 for a specific glycan length. These findings led us to the optimization of combinatorial one‐pot synthesis by variation of substrate and enzyme ratios, as well as starting the synthesis with various poly‐LacNAc chain lengths. Consequently, we present here an optimized poly‐LacNAc synthesis by the combination of two glycosyltransferases and a uridine‐diphospho‐glucose/N‐acetylglucosamine 4′‐epimerase as one‐pot strategy resulting in long poly‐LacNAc glycans with up to six LacNAc units in high yields while minimizing reaction time and product loss. The obtained products are important ligands for the biofunctionalization of biomaterial surfaces and the construction of an artificial extracellular matrix for tissue engineering.

  DOI：

  10.1002/adsc.201100375