| 1393688-23-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• CAS: 1393688-23-7
• 化学式: C₈₉H₁₃₄N₄O₆₀
• 分子量: 2220.03
• InChiKey: OABXZODXRMBDHL-XCPGJWRDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -22.19
• 重原子数：
  153.0
• 可旋转键数：
  40.0
• 环数：
  14.0
• sp3杂化的碳原子比例：
  0.81
• 拓扑面积：
  1004.12
• 氢给体数：
  37.0
• 氢受体数：
  59.0

反应信息

• 作为反应物：
  描述：

  在 Endo H 、 水 作用下， 生成 Man9GlcNAc
  参考文献：
  名称：

  ER葡萄糖基转移酶（UGGT）的依赖于聚糖的重折叠活性。

  摘要：

  背景 在内质网（ER）中，糖蛋白的折叠是由酶和分子伴侣的联合作用来辅助的，从而使糖蛋白折叠成生物功能结构。在该系统中，UDP-葡萄糖：糖蛋白葡萄糖基转移酶1（UGGT1）由于能够区分客户糖蛋白的折叠状态，因此起“折叠传感器”的作用。但是，除了其转移酶活性外，UGGT1是否具有任何有助于蛋白折叠的分子伴侣活性还没有得到解决。 方法 我们使用M9GN-恶唑啉和聚糖截短的RNase B通过化学酶法制备了低聚甘露糖型聚糖修饰的RNase（M9GN2-RNase），并分析了人UGGT1（HUGT1）对变性M9GN2-RNase折叠的影响。基于通过RNA底物的裂解测量的RNase活性评估重折叠。 结果 HUGT1在相同程度上略微加快了M9GN2-RNase和非糖基化RNase A的折叠。但是，HUGT1在UDP-Glc的存在下显着加速了M9GN2-RNase的折叠。相反，UDP和UDP-Gal都不能有

  DOI：

  10.1016/j.bbagen.2020.129709
• 作为产物：
  描述：

  9-芴甲基-N-琥珀酰亚胺基碳酸酯 、 Man9GlcNAc2Asn 在 碳酸氢钠 作用下， 以 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 4.0h， 以40 mg的产率得到
  参考文献：
  名称：

  Efficient synthesis of glycopeptide-α-thioesters with a high-mannose type oligosaccharide by means of tert-Boc-solid phase peptide synthesis

  摘要：

  High-mannose type oligosaccharides consist of nine mannose and two N-acetylglucosamine residues (Man(9)GlcNAc(2):M9) and play an important role in protein folding processes in the endoplasmic reticulum. A highly efficient preparation method of this asparaginyl-M9-oligosaccharide from hen egg yolk was established by a two-step proteolysis with commercially available proteases and subsequent purification using high performance liquid chromatography (HPLC). To avoid the hydrolysis of the desired M9-oligosaccharide during the proteolysis steps, several commercially available proteases were screened for their contamination with mannosidases. The alpha-amino group of the resultant H2N-Asn-(M9-oligosaccharide)OH was protected with 9-fluorenylmethyloxycarbonyl (Fmoc) group for convenient separation by HPLC. The structure of Fmoc-Asn-(M9-oligosaccharide)-OH thus obtained was confirmed by ESI-MS spectrometry and several NMR experiments. Using this Fmoc-Asn-(M9-oligosaccharide)-OH, the synthesis of the M9-glycopeptide-alpha-thioester was demonstrated by means of tert-Boc-solid phase peptide synthesis. These tert-Boc conditions afforded the M9-glycopeptide-alpha-thioester in moderate yield. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2012.10.011

文献信息

• Monitoring of Glycoprotein Quality Control System with a Series of Chemically Synthesized Homogeneous Native and Misfolded Glycoproteins
  作者：Tatsuto Kiuchi、Masayuki Izumi、Yuki Mukogawa、Arisa Shimada、Ryo Okamoto、Akira Seko、Masafumi Sakono、Yoichi Takeda、Yukishige Ito、Yasuhiro Kajihara

  DOI：10.1021/jacs.8b08653

  日期：2018.12.19

  The glycoprotein quality control (GQC) system in the endoplasmic reticulum (ER) effectively uses chaperone-type enzymes and lectins such as UDP-glucose:glycoprotein glucosyltransferase (UGGT), calnexin (CNX), calreticulin (CRT), protein disulfide bond isomerases (ERp57 or PDIs), and glucosidases to generate native-folded glycoproteins from nascent glycopolypeptides. However, the individual processes of the GQC system at the molecular level are still unclear. We chemically synthesized a series of several homogeneous glycoproteins bearing M9-high-mannose type oligosaccharides (M9-glycan), such as erythropoietin (EPO), interferon-beta (IFN-beta), and interleukin 8 (IL8) and their misfolded counterparts, and used these glycoprotein probes to better understand the GQC process. The analyses by high performance liquid chromatography and mass spectrometer clearly showed refolding processes from synthetic misfolded glycoproteins to native form through folding intermediates, allowing for the relationship between the amount of glucosylation and the refolding of the glycoprotein to be estimated. The experiment using these probes demonstrated that GQC system isolated from rat liver acts in a catalytic cycle regulated by the fast crosstalk of glucosylation/deglucosylation in order to accelerate refolding of misfolded glycoproteins.