| 1078153-34-0

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• CAS: 1078153-34-0
• 化学式: C₄₁H₅₄N₄O₂₀
• 分子量: 922.895
• InChiKey: HTZFLDLCXGCXSU-LVOJHCFPSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.78
• 重原子数：
  65.0
• 可旋转键数：
  16.0
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.59
• 拓扑面积：
  370.92
• 氢给体数：
  13.0
• 氢受体数：
  19.0

反应信息

• 作为产物：
  描述：

  、 Fmoc-Asn(GlcNAc)-OH 在 Bacillus sp. chitinase 100 kDa 作用下， 反应 8.0h， 以55%的产率得到
  参考文献：
  名称：

  Chemoenzymatic synthesis of N-linked neoglycoproteins through a chitinase-catalyzed transglycosylation

  摘要：

  A novel application of the Bacillus sp. chitinase for the chemoenzymatic synthesis of N-linked neoglycoproteins is described. Three chitinases with different molecular size were purified from the crude chitinase preparation. The purified chitinases were evaluated for their hydrolytic and transglycosylation activity. One chitinase with a molecular size of 100 kDa (Chi100) was identified to be the one with highest transglycosylation/ hydrolysis ratio. Chi100 could effectively recognize LacNAc-oxazoline and Man alpha 1,3Glc beta 1,4GlcNAc-oxazoline as the donor substrate to glycosylate Asn-linked GlcNAc, while it was unable to recognize Man beta 1,4GlcNAc and Man(3)GlcNAc-oxazolines as the donor substrates. The chitinase-catalyzed transglycosylation was successfully extended to the remodeling of ribonuclease B to afford neoglycoproteins. Although the yield needs to be optimized, the chitinase-catalyzed transglycosylation provides a potentially useful tool for the synthesis of neoglycoproteins carrying novel N-linked oligosaccharides. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.08.042

文献信息

• Spore-Encapsulating Glycosyltransferase Catalysis Tandem Reactions: Facile Chemoenzymatic Synthesis of Complex Human Glycans
  作者：Qiang Chao、Tianlu Li、Ji-Xiang Jia、Zijie Li、Peng Peng、Xiao-Dong Gao、Ning Wang

  DOI：10.1021/acscatal.1c05630

  日期：2022.3.4

  encapsulated on the surface of yeast spores, which enabled facile assembly of diverse naturally occurring sialyl-galactosylated glycans, including human milk oligosaccharide, N-glycan biomarker, O-Man glycan, and O-GalNAc glycan. The utility of this strategy was further demonstrated by systematic construction of a panel of Core 2 O-GalNAc glycans.

  唾液酸半乳糖 (Sia-Gal) 是寡糖最丰富的末端基序之一，广泛存在于动物的糖缀合物和未缀合聚糖中。为了研究它们的功能和生物学作用，必须获得末端结构确定的寡糖。在此，我们描述了一种使用固定化酶对具有末端半乳糖 (Gal) 或 Sia-Gal 残基的聚糖进行区域选择性修饰的便捷有效策略。半乳糖基转移酶 (GalT) 和唾液酸转移酶 (ST) 被包裹在酵母孢子的表面，这使得多种天然存在的唾液酸-半乳糖基化聚糖（包括人乳寡糖、N-聚糖生物标志物、O -Man聚糖和O-GalNAc聚糖。通过系统构建一组核心 2 O -GalNAc 聚糖进一步证明了该策略的实用性。