(5-acetamido-3,5-dideoxy-α-D-glycero-D-galacto-2-nonulopyranosylonic acid)-(2-3)-β-D-galactopyranosyl-(1-4)-α,β-D-glucopyranose | 64839-33-4

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (5-acetamido-3,5-dideoxy-α-D-glycero-D-galacto-2-nonulopyranosylonic acid)-(2-3)-β-D-galactopyranosyl-(1-4)-α,β-D-glucopyranose
• 英文别名: alpha-NeuAc-(2->3)-beta-D-Gal-(1->4)-D-Glc(1-)；(2S,4S,5R,6R)-5-acetamido-2-[(2R,3S,4S,5R,6S)-3,5-dihydroxy-2-(hydroxymethyl)-6-[(2R,3S,4R,5R)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-4-yl]oxy-4-hydroxy-6-[(1R,2R)-1,2,3-trihydroxypropyl]oxane-2-carboxylate
• CAS: 64839-33-4
• 化学式: C₂₃H₃₈NO₁₉
• 分子量: 632.55
• InChiKey: CILYIEBUXJIHCO-METZQCMUSA-M

物化性质

• 沸点：
  1134.9±65.0 °C(Predicted)
• 密度：
  1.77±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -6.6
• 重原子数：
  43
• 可旋转键数：
  10
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.91
• 拓扑面积：
  338
• 氢给体数：
  12
• 氢受体数：
  19

反应信息

• 作为反应物：
  描述：

  N-methyl-O-benzylhydroxylamine hydrochloride 、 (5-acetamido-3,5-dideoxy-α-D-glycero-D-galacto-2-nonulopyranosylonic acid)-(2-3)-β-D-galactopyranosyl-(1-4)-α,β-D-glucopyranose 在 sodium acetate 作用下， 以 水 为溶剂， 以91 %的产率得到
  参考文献：
  名称：

  唾液酸化寡糖的 N-甲基-O-苄基羟胺衍生物、其合成和反相 HPLC 分离

  摘要：

  将人乳三糖 3'- 唾液酸乳糖与过量的 N-甲基-O-苄基羟胺 (MBHA) 反应，通过固相萃取以高产率 (91%) 分离出产物 3'- 唾液酸乳糖-MBHA。还制备了异构三糖 6'-唾液酸乳糖-MBHA，在本例中是通过乳糖-MBHA 的酶促唾液酸化来制备的。两种唾液酸乳糖-MBHA 衍生物的 50/50 混合物可以通过反相 HPLC 轻松分离。通过酸水解从它们各自的MBHA衍生物中回收游离寡糖。

  DOI：

  10.1016/j.carres.2023.108939
• 作为产物：
  描述：

  在 水 作用下， 以90 %的产率得到(5-acetamido-3,5-dideoxy-α-D-glycero-D-galacto-2-nonulopyranosylonic acid)-(2-3)-β-D-galactopyranosyl-(1-4)-α,β-D-glucopyranose
  参考文献：
  名称：

  唾液酸化寡糖的 N-甲基-O-苄基羟胺衍生物、其合成和反相 HPLC 分离

  摘要：

  将人乳三糖 3'- 唾液酸乳糖与过量的 N-甲基-O-苄基羟胺 (MBHA) 反应，通过固相萃取以高产率 (91%) 分离出产物 3'- 唾液酸乳糖-MBHA。还制备了异构三糖 6'-唾液酸乳糖-MBHA，在本例中是通过乳糖-MBHA 的酶促唾液酸化来制备的。两种唾液酸乳糖-MBHA 衍生物的 50/50 混合物可以通过反相 HPLC 轻松分离。通过酸水解从它们各自的MBHA衍生物中回收游离寡糖。

  DOI：

  10.1016/j.carres.2023.108939

文献信息

• Molecular insight into substrate recognition by human cytosolic sialidase NEU2
  作者：Alessandra Mozzi、Pietro Mazzacuva、Giuseppe Zampella、Matilde Emma Forcella、Paola Alessandra Fusi、Eugenio Monti

  DOI：10.1002/prot.24013

  日期：2012.4

  structure represents a pivotal step toward the characterization of the molecular basis of natural substrates recognition by the enzyme. In this perspective, we have carried out a study of molecular docking of NEU2 active site using natural substrates of increasing complexity. Moreover, selective mutations of the residues putatively involved into substrate(s) interaction/recognition have been performed

  唾液酸酶或神经酰胺酶是糖苷水解酶，可去除唾液糖蛋白和唾液糖脂中的末端唾液酸残基。病毒神经氨酸酶（NAs）已被广泛表征，并通过合成一系列竞争性抑制剂来阻断抗病毒治疗的出色靶点，这些抑制剂可阻止新形成的病毒颗粒从感染细胞中释放。人胞浆唾液酸酶NEU2是唯一在结构上表征的哺乳动物酶，它代表了研究新型NA抑制药物特异性的有价值的模型。此外，NEU2 3D结构的可用性代表了表征酶识别天然底物的分子基础的关键步骤。从这个角度来看，我们已经使用越来越复杂的天然底物进行了NEU2活性位点的分子对接研究。此外，已经进行了假定参与底物相互作用/识别的残基的选择性突变，并且已经初步测试了所得的突变酶的催化活性和底物特异性。我们发现Q270参与了二糖α（2,3）唾液酸半乳糖的结合，而K45和Q112结合了三糖α（2,3）唾液酸乳糖的远端葡萄糖，对应于GM3的寡糖部分神经节苷脂。此外，除D46外，E218被证明是关
• Structural Insights into the Broad Substrate Specificity of a Novel Endoglycoceramidase I Belonging to a New Subfamily of GH5 Glycosidases
  作者：Yun-Bin Han、Liu-Qing Chen、Zhuo Li、Yu-Meng Tan、Yan Feng、Guang-Yu Yang

  DOI：10.1074/jbc.m116.763821

  日期：2017.3

  the strict substrate specificity of these GH5 glycosidases has not been identified. In this study, we report a novel EGCase I from Rhodococcus equi 103S (103S_EGCase I) with remarkably broad substrate specificity. Based on phylogenetic analyses, the enzyme may represent a new subfamily of GH5 glycosidases. The X-ray crystal structures of 103S_EGCase I alone and in complex with its substrates monosial

  内切糖苷酰胺酶（EGCases）特异性水解各种糖鞘脂的寡糖和神经酰胺部分之​​间的糖苷键，并且它们在糖鞘脂学的新兴领域中受到了广泛的关注。然而，尚未确定调节这些GH5糖苷酶的严格底物特异性的机制。在这项研究中，我们报告了一种新的EGCase I，它来自Rhodococcus equi 103S（103S_EGCase I），具有广泛的底物特异性。基于系统发育分析，该酶可能代表了GH5糖苷酶的一个新的亚家族。103S_EGCase I的X射线晶体结构及其与底物单唾液酸二己糖基神经节苷脂（GM3）和单唾液酸四己糖基神经节苷脂（GM1）的复合物使我们能够鉴定出可能解释其广泛特异性的几个结构特征。与来自红球菌属的EGCase II比较。M-777（M777_EGCase II）具有严格的底物特异性，103S_EGCase I具有较长的alpha7-螺旋和较短的loop4，后者形成了较大的底物结合袋
• Properties of Recombinant Human Cytosolic Sialidase HsNEU2
  作者：Cristina Tringali、Nadia Papini、Paola Fusi、Gianluigi Croci、Giuseppe Borsani、Augusto Preti、Paolo Tortora、Guido Tettamanti、Bruno Venerando、Eugenio Monti

  DOI：10.1074/jbc.m308381200

  日期：2004.1

  Recombinant human cytosolic sialidase (HsNEU2), expressed in Escherichia coli, was purified to homogeneity, and its substrate specificity was studied. HsNEU2 hydrolyzed 4-methylumbelliferyl alpha-NeuAc, alpha2-->3 sialyl-lactose, glycoproteins (fetuin, alpha-acid glycoprotein, transferrin, and bovine submaxillary gland mucin), micellar gangliosides GD1a, GD1b, GT1b, and alpha2-->3 paragloboside, and vesicular GM3. alpha2-->6 sialyllactose, colominic acid, GM1 oligosaccharide, whereas micellar GM2 and GM1 were resistant. The optimal pH was 5.6, kinetics Michaelis-Menten type, V-max varying from 250 IU/mg protein (GD1a) to 0.7 IU/mg protein (alpha(1)-acid glycoprotein), and K-m in the millimolar range. HsNEU2 was activated by detergents (Triton X-100) only with gangliosidic substrates; the change of GM3 from vesicular to mixed micellar aggregation led to a 8.5-fold V-max increase. HsNEU2 acted on gangliosides (GD1a, GM1, and GM2) at nanomolar concentrations. With these dispersions (studied in detailed on GM1), where monomers are bound to the tube wall or dilutedly associated (1:2000, mol/mol) to Triton X-100 micelles, the V-max values were 25 and 72 muIU/mg protein, and K-m was 10 and 15x10(-9) M, respectively. Remarkably, GM1 and GM2 were recognized only as monomers. HsNEU2 worked at pH 7.0 with an efficiency (compared with that at pH 5.6) ranging from 4% (on GD1a) to 64% (on alpha(1)-acid glycoprotein), from 7% (on GD1a) to 45% (on GM3) in the presence of Triton X-100, and from 30 to 40% on GM1 monomeric dispersion. These results show that HsNEU2 differentially recognizes the type of sialosyl linkage, the aglycone part of the substrate, and the supramolecular organization (monomer/micelle/vesicle) of gangliosides. The last ability might be relevant in sialidase interactions with gangliosides under physiological conditions.
• N-methyl-O-benzylhydroxylamine derivatives of sialylated oligosaccharides, their synthesis and separation with reversed-phase HPLC
  作者：Thomas Norberg、Elisabet Kallin

  DOI：10.1016/j.carres.2023.108939

  日期：2023.11

  isomeric trisaccharide 6′-sialyllactose-MBHA was also prepared, in this case by enzymatic sialylation of lactose-MBHA. A 50/50 mixture of the two sialyllactose-MBHA derivatives was easily separated by reversed-phase HPLC. The free oligosaccharides were recovered from their respective MBHA derivatives by acid hydrolysis.

  将人乳三糖 3'- 唾液酸乳糖与过量的 N-甲基-O-苄基羟胺 (MBHA) 反应，通过固相萃取以高产率 (91%) 分离出产物 3'- 唾液酸乳糖-MBHA。还制备了异构三糖 6'-唾液酸乳糖-MBHA，在本例中是通过乳糖-MBHA 的酶促唾液酸化来制备的。两种唾液酸乳糖-MBHA 衍生物的 50/50 混合物可以通过反相 HPLC 轻松分离。通过酸水解从它们各自的MBHA衍生物中回收游离寡糖。