| 1078153-35-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• CAS: 1078153-35-1
• 化学式: C₄₇H₆₄N₄O₂₅
• 分子量: 1085.04
• InChiKey: GYOKOUMCHCXCMQ-KALZYNFUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -6.96
• 重原子数：
  76.0
• 可旋转键数：
  19.0
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.64
• 拓扑面积：
  450.07
• 氢给体数：
  16.0
• 氢受体数：
  24.0

反应信息

• 作为产物：
  描述：

  α-Man-(1->3)-β-Glcp-(1->4)-GlcpNAc 、 Fmoc-Asn(GlcNAc)-OH 在 endo-β-N-acetylglucosaminidase 作用下， 以 phosphate buffer 为溶剂， 反应 24.0h， 以43%的产率得到
  参考文献：
  名称：

  Endo-β-N-acetylglucosaminidase-catalyzed polymerization of β-Glcp-(1→4)-GlcpNAc oxazoline: a revisit to enzymatic transglycosylation

  摘要：

  An alternative synthesis of beta-Glcp-(1 -> 4)-GlcpNAc oxazoline is described, and its enzymatic reaction with the endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae (Endo-A) was re-investigated. Under normal transglycosylation conditions with a catalytic amount of enzyme, Enclo-A showed only marginal activity for transglycosylation with the disaccharide oxazoline, consistent with our previous observations. However, when used in a relatively large quantity, Endo-A could promote the transglycosylation of the disaccharide oxazoline to a GlcpNAc-Asn acceptor. In addition to the initial transglycosylation product, a series of large oligosaccharides were also formed due to the tandem transglycosylation to the terminal glucose residues in the intermediate products. In the absence of an external acceptor, Enclo-A could polymerize the disaccharide oxazoline to form oligo- and polysaccharides having the -4-beta-(Glcp-(1 -> 4)-beta-GlcpNAc)-1-repeating units. This is the first example of an endo-beta-N-acetylglucosaminidase-promoted polymerization of activated oligosaccharide substrates. This enzymatic polymerization may find useful applications for the synthesis of novel artificial polysaccharides. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2009.01.016

文献信息

• Chemoenzymatic synthesis of N-linked neoglycoproteins through a chitinase-catalyzed transglycosylation
  作者：Cishan Li、Wei Huang、Lai-Xi Wang

  DOI：10.1016/j.bmc.2008.08.042

  日期：2008.9

  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.