β1,1-galactopyranosyl xylopyranoside

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: β1,1-galactopyranosyl xylopyranoside
• 英文别名: (2R,3R,4S,5R,6S)-2-(hydroxymethyl)-6-[(2S,3R,4S,5R)-3,4,5-trihydroxyoxan-2-yl]oxyoxane-3,4,5-triol
• 化学式: C₁₁H₂₀O₁₀
• 分子量: 312.274
• InChiKey: FWHMSYJZNKVPEG-MRRNQDDQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.1
• 重原子数：
  21
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  169
• 氢给体数：
  7
• 氢受体数：
  10

反应信息

• 作为产物：
  描述：

  尿苷(5')二氢二磷酰(1)-alpha-D-葡萄糖 生成 β1,1-galactopyranosyl xylopyranoside
  参考文献：
  名称：

  Xylose: The First Ambident Acceptor Substrate for Galactosyltransferase from Bovine Milk

  摘要：

  In the past few years the acceptor substrate specificity of beta 1,4-galactosyltransferase (GalT) from bovine milk has been investigated extensively by various groups. In each case, the beta 1,4-galactosylated products have been observed exclusively. Recently we reported on a frame-shifted recognition of modified acceptor substrates resulting in the formation of beta,beta-trehalose type disaccharides. In an extension to these investigations we have now found that xylose is recognized by the enzyme both in the normal and in the reverse orientation. Therefore galactosylation of xylose results in a mixture of beta 1,4- and beta 1,beta 1-galactopyranosyl xylopyranosides. Synthesis and preparation of both disaccharides and their behavior toward beta-galactosidase from E. coli are described. The results lead to some implications about the active site of GalT.

  DOI：

  10.1021/jo00101a038

文献信息

• Stereoselective enzymatic galactosylation of C-glucosides
  作者：Luigi Panza、Pietro L. Chiappini、Giovanni Russo、Daniela Monti、Sergio Riva

  DOI：10.1039/a701747b

  日期：——

  The enzyme β-1,4-galactosyl transferase from bovine colostrum (GalT) is able stereoselectively to galactosylate C-glucosides (i.e. 1 and 4), precursors of stable glycoconjugate analogues, and a systematic investigation of the structural modifications at C-1 and/or C-5 of the glycosides that can be accepted by this enzyme has been undertaken, adding information to the currently accepted model of substrate binding into the GalT active site.

  牛初乳中的β-1,4-半乳糖基转移酶（GalT）能够立体选择性地半乳糖基化C-葡萄糖苷（即1和4）--稳定的糖苷类似物的前体--并对该酶可接受的糖苷的C-1和/或C-5结构修饰进行了系统研究，为目前公认的底物结合到GalT活性位点的模型增添了信息。
• Xylose: The First Ambident Acceptor Substrate for Galactosyltransferase from Bovine Milk
  作者：Torsten Wiemann、Yoshihiro Nishida、Volker Sinnwell、Joachim Thiem

  DOI：10.1021/jo00101a038

  日期：1994.11

  In the past few years the acceptor substrate specificity of beta 1,4-galactosyltransferase (GalT) from bovine milk has been investigated extensively by various groups. In each case, the beta 1,4-galactosylated products have been observed exclusively. Recently we reported on a frame-shifted recognition of modified acceptor substrates resulting in the formation of beta,beta-trehalose type disaccharides. In an extension to these investigations we have now found that xylose is recognized by the enzyme both in the normal and in the reverse orientation. Therefore galactosylation of xylose results in a mixture of beta 1,4- and beta 1,beta 1-galactopyranosyl xylopyranosides. Synthesis and preparation of both disaccharides and their behavior toward beta-galactosidase from E. coli are described. The results lead to some implications about the active site of GalT.