3,4,6-tri-O-acetyl-2-deoxy-2-trifluoroacetylamino-α-D-glucopyranosyl dibenzyl phosphate | 219564-51-9

• 分子结构分类: 有机化合物 - 有机酸及其衍生物
• 英文名称: 3,4,6-tri-O-acetyl-2-deoxy-2-trifluoroacetylamino-α-D-glucopyranosyl dibenzyl phosphate
• 英文别名: [(2R,3S,4R,5R,6R)-3,4-diacetyloxy-6-bis(phenylmethoxy)phosphoryloxy-5-[(2,2,2-trifluoroacetyl)amino]oxan-2-yl]methyl acetate
• CAS: 219564-51-9
• 化学式: C₂₈H₃₁F₃NO₁₂P
• 分子量: 661.523
• InChiKey: OFIPBBWHIUYLGE-ZFXZZAOISA-N

物化性质

• 沸点：
  706.2±60.0 °C(Predicted)
• 密度：
  1.40±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.74
• 重原子数：
  45.0
• 可旋转键数：
  13.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  161.99
• 氢给体数：
  1.0
• 氢受体数：
  12.0

反应信息

• 作为反应物：
  描述：

  3,4,6-tri-O-acetyl-2-deoxy-2-trifluoroacetylamino-α-D-glucopyranosyl dibenzyl phosphate 在 palladium on activated charcoal 氢气 作用下， 以 甲醇 为溶剂， 反应 2.5h， 生成 2-deoxy-2-[(trifluoroacetyl)amino]-D-glucopyranose-3,4,6-triacetate-1-(dihydrogen phosphate)
  参考文献：
  名称：

  O-GlcNAc转移酶抑制剂的发现

  摘要：

  丝氨酸和苏氨酸残基的 O-GlcNAcylation 是一种动态且必不可少的翻译后修饰，涉及真核生物的信号通路。O-GlcNAc 转移酶 (OGT) 的小分子抑制剂将有助于 O-GlcNAc 酰化的研究，O-GlcNAc 转移酶是已知介导这种修饰的唯一酶，但由于克隆 OGT 表达不佳和缺乏合适的高- 吞吐量屏幕。该通讯描述了一种表达系统的开发，以访问大量 OGT 的催化结构域，以及基于荧光的底物类似物置换分析的实施，从而发现了一组 OGT 抑制剂。这项工作为 OGT 催化域的结构和功能分析奠定了基础。

  DOI：

  10.1021/ja0555217
• 作为产物：
  描述：

  3,4,6-tri-O-acetyl-2-deoxy-2-trifluoroacetamido-α-D-glucospyranosyl bromide 在 2,6-二甲基吡啶 作用下， 以 1,2-二氯乙烷 、 乙腈 为溶剂， 反应 1.0h， 生成 3,4,6-tri-O-acetyl-2-deoxy-2-trifluoroacetylamino-α-D-glucopyranosyl dibenzyl phosphate
  参考文献：
  名称：

  方便合成α-和β-d-葡糖胺-1-磷酸及其衍生物

  摘要：

  α-和β-d-氨基葡萄糖-1-磷酸酯的衍生物以及α-d-半乳糖胺-1-磷酸酯以及游离的β-d-氨基葡萄糖-1-磷酸酯的衍生物通过立体选择性地制备。衍生自相应的3,4,6-三-O-乙酰基-2-脱氧-2-三氟乙酰胺基-α-d-己基吡喃糖基溴化物与磷酸二苄酯的1，2-恶唑啉的开口。

  DOI：

  10.1016/s0040-4039(98)01838-3

文献信息

• Chemoenzymatic synthesis of thio-nod factor intermediates — Enzymatic transfer of glucosamine on thiochitobiose derivatives
  作者：Latino Loureiro Morais、Hideya Yuasa、Khalil Bennis、Isabelle Ripoche、France-Isabelle Auzanneau

  DOI：10.1139/v06-043

  日期：2006.4.1

  The chemoenzymatic syntheses of thioanalogues of nodulation factors in which the nonreducing end glucosamine residue is available for the introduction of the fatty acid moiety at the free NH₂group are reported. We are describing the chemical synthesis of UDP-GlcNH₂and its use in the enzymatic transfer of GlcNH₂by the bovine galactosyltransferase (EC 2.4.1.90) onto O-4 of the nonreducing end N-acetylglucosamine residues of chitobiose, thiochitobiose, and allyl thiochitobioside. The enzymatic reactions on chitobiose and thiochitobiose were followed by TLC and MALDI MS and showed about 50% conversion of the disaccharides to the desired products. However, these reducing trisaccharides could not be obtained totally free of salts and degraded on ion exchange chromatography. Thus, we investigated the enzymatic transfer on the nonreducing allyl thiochitobioside analogue. We describe here the chemical synthesis of this thiodisaccharide and the enzymatic transfer of GlcNH₂at O-4 of its nonreducing end glucosamine residue to give the desired allyl thiotrisaccharide. This thiotrisaccharide was obtained pure in 41% yield and was characterized by¹H NMR (HSQC) and HRMS.Key words: nodulation factors, synthesis, enzymatic transfer, thiooligosaccharides, UDP-glucosamine.

  本研究报道了用化学酶法合成结瘤因子硫代类似物的过程，在这些类似物中，非还原端葡糖胺残基可用于在游离 NH2 基上引入脂肪酸分子。我们介绍了 UDP-GlcNH2 的化学合成及其在牛半乳糖基转移酶（EC 2.4.1.90）将 GlcNH2 酶促转移到壳寡糖、硫代壳寡糖和烯丙基硫代壳寡糖的非还原端 N-乙酰葡糖胺残基的 O-4 上的应用。利用 TLC 和 MALDI MS 对壳寡糖和硫代壳寡糖的酶促反应进行了跟踪，结果表明这些二糖约有 50% 转化为所需产物。然而，这些还原性三糖不能完全不含盐分，并在离子交换色谱中降解。因此，我们研究了非还原性烯丙基硫代几丁质类似物的酶促转移。我们在此描述了这种硫代二糖的化学合成及其非还原端氨基葡萄糖残基 O-4 上 GlcNH2 的酶促转移，从而得到所需的烯丙基硫代三糖。这种硫代异糖的纯度为 41%，并通过 1H NMR (HSQC) 和 HRMS 进行了表征。
• Substrate specificity of N-acetylglucosaminyl(diphosphodolichol) N-acetylglucosaminyl transferase, a key enzyme in the dolichol pathway
  作者：V Tai

  DOI：10.1016/s0968-0896(00)00334-5

  日期：2001.5

  N-Acetylglucosaminyl(diphosphodolichol) N-acetylglucosaminyl transferase, also known as Enzyme II, is the second enzyme in the dolichol pathway. This pathway is responsible for the assembly of the tetradecasaccharide pyrophosphate dolichol, which is the substrate for oligosaccharyl transferase. In order to study the specificity of Enzyme II, four unnatural dolichol diphosphate monosaccharides were synthesized, with the C-2 acetamido group in the natural substrate Dol-PP-GlcNAc la replaced by fluoro, ethoxy, trifluoroacetamido, and amino functionalities. These analogues Ib-e were evaluated as glycosyl accepters for Enzyme II, which catalyzes the formation of dolichol diphosphate chitobiose (Dol-PP-GlcNAc(2)) from UDP-GlcNAc and Dol-PP-GlcNAc. Enzyme II from pig liver was found to be highly specific for its glycosyl acceptor and the acetamido group shown to be a key functional determinant for this glycosylation reaction. (C) 2001 Elsevier Science Ltd. All rights reserved.