N-acetylglucosamine-6-sulphate | 10356-99-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: N-acetylglucosamine-6-sulphate
• 英文别名: N-acetyl-β-D-glucosamine-6-O-sulfate；GlcNAc-6S；2-acetamido-2-deoxy-6-O-sulfo-beta-D-glucopyranose；[(2R,3S,4R,5R,6R)-5-acetamido-3,4,6-trihydroxyoxan-2-yl]methyl hydrogen sulfate
• CAS: 10356-99-7
• 化学式: C₈H₁₅NO₉S
• 分子量: 301.274
• InChiKey: WJFVEEAIYIOATH-FMDGEEDCSA-N

物化性质

• 熔点：
  120 °C (decomp)
• 密度：
  1.648±0.06 g/cm3(Predicted)
• 物理描述：
  Solid

计算性质

• 辛醇/水分配系数(LogP)：
  -3.5
• 重原子数：
  19
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  171
• 氢给体数：
  5
• 氢受体数：
  9

反应信息

• 作为产物：
  描述：

  2-乙酰氨基-2-脱氧-beta-D-吡喃葡萄糖胺 在 carbohydrate sulfotransferase 2 、 6-氨基-9-[3-羟基-5-[(羟基-磺基氧基-磷酰)氧基甲基]-4-膦酰氧基-四氢呋喃-2-基]-嘌呤 作用下， 生成 N-acetylglucosamine-6-sulphate
  参考文献：
  名称：

  Detecting O-GlcNAc using in vitro sulfation

  摘要：

  O-链接β-N-乙酰葡萄糖胺（O-GlcNAc）糖基化是N-乙酰葡萄糖胺与蛋白质中的丝氨酸和苏氨酸残基共价结合的一种翻译后修饰，与蛋白质磷酸化有许多共同特征。O-GlcNAc对于细胞存活至关重要，在许多生物过程（如转录、翻译、细胞分裂）和人类疾病（如糖尿病、阿尔茨海默病、癌症）中发挥着重要作用。然而，检测O-GlcNAc具有挑战性。本文介绍了一种使用体外硫酸化结合两种N-乙酰葡萄糖胺（GlcNAc）特异性硫酸转移酶（碳水化合物硫酸转移酶2和碳水化合物硫酸转移酶4）和放射性同位素35S来检测O-GlcNAc的方法。首先证明了游离GlcNAc的硫酸化，然后证明了肽以及核蛋白和细胞质蛋白中O-GlcNAc残基的硫酸化。还证明了O-GlcNAc的硫酸化对OGT和O-β-N-乙酰葡萄糖胺酶处理敏感。标记的样品在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳中分离，并通过自动放射成像进行可视化。总体而言，该方法灵敏、特异且方便。

  DOI：

  10.1093/glycob/cwu037

文献信息

• Sulphated Mucin Oligosaccharides from Porcine Small Intestine Analysed by Four-Sector Tandem Mass Spectrometry
  作者：Niclas G. Karlsson、Hasse Karlsson、Gunnar C. Hansson

  DOI：10.1002/(sici)1096-9888(199605)31:5<560::aid-jms331>3.0.co;2-0

  日期：1996.5

  The fraction of sulphated oligosaccharide alditols isolated from mucin glycopeptides of porcine small intestine 'insoluble' mucin complex was analysed by negative-ion fast atom bombardment (FAB) tandem mass spectrometry. Collision-induced dissociation (CID) tandem mass spectra of native and peracetylated species were compared with standards of sulphated monosaccharides. The tandem mass spectra revealed structural information of the carbohydrate sequence and sulphate position. Negative-ion FAB ionization of the peracetylated sulphated oligo-saccharide alditols was at least three times more sensitive than that of the native sulphated oligosaccharide alditols, as revealed by comparing the signal-to-noise ratios, and allowed the detection of eleven compared with six pseudo-molecular ions. Fourteen structures were determined from the CID tandem mass spectra obtained. The main sulphation site was C-6 of an N-acetylglucosamine 6-linked to the N-acetylgalactosaminitol. C-3 of the N-acetylgalactosaminitol could be unsubstituted or extended with a series of up to three monosaccharide residues including blood group H determinants and blood group A determinants. Also, the sulphated N-acetylglucosamine could be further extended. The most abundant structure was a monosulphated trisaccharide with the sequence Gal-->3(SO3-->6GlcNAc-->6)GalNAcol. The sulphation at C-6 of N-acetylglucosamine seems to be a common feature for O-linked oligosaccharides, and has been described both for skeletal keratan sulphates and respiratory mucin oligosaccharides. Low-abundance ions were also detected from oligosaccharides with sulphation at C-3 of an amino sugar residue. This seems to be a novel sulphation site for mucin oligosaccharides.
• Detecting O-GlcNAc using in vitro sulfation
  作者：Zhengliang L Wu、Matthew T Robey、Timothy Tatge、Cheng Lin、Nancy Leymarie、Yonglong Zou、Joseph Zaia

  DOI：10.1093/glycob/cwu037

  日期：2014.8.1

  O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation, the covalent attachment of N-acetylglucosamine to serine and threonine residues of proteins, is a post-translational modification that shares many features with protein phosphorylation. O-GlcNAc is essential for cell survival and plays important role in many biological processes (e.g. transcription, translation, cell division) and human diseases (e.g. diabetes, Alzheimer's disease, cancer). However, detection of O-GlcNAc is challenging. Here, a method for O-GlcNAc detection using in vitro sulfation with two N-acetylglucosamine (GlcNAc)-specific sulfotransferases, carbohydrate sulfotransferase 2 and carbohydrate sulfotransferase 4, and the radioisotope 35S is described. Sulfation on free GlcNAc is first demonstrated, and then on O-GlcNAc residues of peptides as well as nuclear and cytoplasmic proteins. It is also demonstrated that the sulfation on O-GlcNAc is sensitive to OGT and O-β-N-acetylglucosaminidase treatment. The labeled samples are separated on sodium dodecyl sulfate–polyacrylamide gel electrophoresis and visualized by autoradiography. Overall, the method is sensitive, specific and convenient.

  O-链接β-N-乙酰葡萄糖胺（O-GlcNAc）糖基化是N-乙酰葡萄糖胺与蛋白质中的丝氨酸和苏氨酸残基共价结合的一种翻译后修饰，与蛋白质磷酸化有许多共同特征。O-GlcNAc对于细胞存活至关重要，在许多生物过程（如转录、翻译、细胞分裂）和人类疾病（如糖尿病、阿尔茨海默病、癌症）中发挥着重要作用。然而，检测O-GlcNAc具有挑战性。本文介绍了一种使用体外硫酸化结合两种N-乙酰葡萄糖胺（GlcNAc）特异性硫酸转移酶（碳水化合物硫酸转移酶2和碳水化合物硫酸转移酶4）和放射性同位素35S来检测O-GlcNAc的方法。首先证明了游离GlcNAc的硫酸化，然后证明了肽以及核蛋白和细胞质蛋白中O-GlcNAc残基的硫酸化。还证明了O-GlcNAc的硫酸化对OGT和O-β-N-乙酰葡萄糖胺酶处理敏感。标记的样品在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳中分离，并通过自动放射成像进行可视化。总体而言，该方法灵敏、特异且方便。