N-acetyl-D-galactosamine 6-O-sulfate

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: N-acetyl-D-galactosamine 6-O-sulfate
• 英文别名: [(2R,3R,4R,5R)-5-acetamido-3,4,6-trihydroxyoxan-2-yl]methyl sulfate
• 化学式: C8H14NO9S-
• 分子量: 300.27
• InChiKey: WJFVEEAIYIOATH-KEWYIRBNSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -3.6
• 重原子数：
  19
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  174
• 氢给体数：
  4
• 氢受体数：
  9

反应信息

• 作为产物：
  描述：

  水 、 oligosaccharide C6S-3 生成 alpha-L-iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine 、 N-acetyl-D-galactosamine 6-O-sulfate
  参考文献：
  名称：

  Physiological Substrates for Human Lysosomal β-Hexosaminidase S

  摘要：

  Human lysosomal beta-hexosaminidases remove terminal beta-glycosidically bound N-acetylhexosamine residues from a number of glycoconjugates. Three different isozymes composed of two noncovalently linked sub-units alpha and beta exist: Hex A (alphabeta), Hex B (betabeta), and Hex S (alphaalpha). While the role of Hex A and B for the degradation of several anionic and neutral glycoconjugates has been well established, the physiological significance of labile Hex S has remained unclear. However, the striking accumulation of anionic oligosaccharides in double knockout mice totally deficient in hexosaminidase activity but not in mice expressing Hex S (Sango, K., McDonald, M. P., Crawley, J. N., Mack, M. L., Tifft, C.J., Skop, E., Starr, C. M., Hoffmann, A., Sandhoff, K., Suzuki, K., and Proia, R. L., (1996) Nat. Genet. 14, 348-352) prompted us to reinvestigate the substrate specificity of Hex S. To identify physiological substrates of Hex S, anionic and neutral oligosaccharides excreted in the urine of the double knockout mice were isolated and analyzed. Using ESI-MS/MS and glycosidase digestion the anionic glycans were identified as products of in. complete dermatan sulfate degradation whereas the neutral storage oligosaccharides were found to be fragments of N-glyean degradation. In vitro, recombinant Hex S was highly active on water-soluble and amphiphilic glycoconjugates including artificial substrates, sulfated GAG fragments, and the sulfated glycosphingolipid SM2. Hydrolysis of membrane-bound SM2 by the recombinant Hex S was synergistically stimulated by the GM2 activator protein and the lysosomal anionic phospholipid bis (monoacylglycero) phosphate.

  DOI：

  10.1074/jbc.m105457200