2-deoxy-2-[(trifluoroacetyl)amino]-D-glucopyranose-3,4,6-triacetate-1-(dihydrogen phosphate) | 212137-46-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 2-deoxy-2-[(trifluoroacetyl)amino]-D-glucopyranose-3,4,6-triacetate-1-(dihydrogen phosphate)
• 英文别名: 3,4,6-tri-O-acetyl-2-deoxy-2-trifluoroacetylamino-α-D-glucopyranosyl phosphate；3,4,6-tri-O-acetyl-2-deoxy-2-trifluoroacetamido-α-D-glucopyranosyl phosphate；TfaNH(-2d)a-Glc1P3Ac4Ac6Ac；[(2R,3S,4R,5R,6R)-3,4-diacetyloxy-6-phosphonooxy-5-[(2,2,2-trifluoroacetyl)amino]oxan-2-yl]methyl acetate
• CAS: 212137-46-7
• 化学式: C₁₄H₁₉F₃NO₁₂P
• 分子量: 481.273
• InChiKey: NKPWIPHJBZXTBV-LZQZFOIKSA-N

物化性质

• 密度：
  1.57±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -1.4
• 重原子数：
  31
• 可旋转键数：
  10
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  184
• 氢给体数：
  3
• 氢受体数：
  15

反应信息

• 作为反应物：
  描述：

  2-deoxy-2-[(trifluoroacetyl)amino]-D-glucopyranose-3,4,6-triacetate-1-(dihydrogen phosphate) 在 sodium cacodylate 、 manganese(ll) chloride ammonium hydroxide 、 bovine milk β-1,4-galactosyltransferase 、 N,N'-羰基二咪唑 、 α-lactalbumin 、 alkaline phosphatase 作用下， 以 甲醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 336048.0h， 生成 4-S-(2-acetamido-4-O-(2-amino-2-deoxy-β-D-glucopyranosyl)-2-deoxy-β-D-glucopyranosyl)-2-acetamido-2-deoxy-4-thio-D-glucopyranose
  参考文献：
  名称：

  Chemoenzymatic synthesis of thio-nod factor intermediates — Enzymatic transfer of glucosamine on thiochitobiose derivatives

  摘要：

  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。

  DOI：

  10.1139/v06-043
• 作为产物：
  描述：

  3,4,6-tri-O-acetyl-2-deoxy-2-trifluoroacetamido-α-D-glucopyranose 在 palladium on activated charcoal 正丁基锂 、 氢气 作用下， 以 四氢呋喃 、 甲醇 、 正己烷 为溶剂， 反应 3.03h， 生成 2-deoxy-2-[(trifluoroacetyl)amino]-D-glucopyranose-3,4,6-triacetate-1-(dihydrogen phosphate)
  参考文献：
  名称：

  Chemoenzymatic synthesis of thio-nod factor intermediates — Enzymatic transfer of glucosamine on thiochitobiose derivatives

  摘要：

  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。

  DOI：

  10.1139/v06-043

文献信息

• Discovery of <i>O-</i>GlcNAc Transferase Inhibitors
  作者：Benjamin J. Gross、Brian C. Kraybill、Suzanne Walker

  DOI：10.1021/ja0555217

  日期：2005.10.1

  essential post-translational modification involved in signaling pathways in eukaryotes. Studies of O-GlcNAcylation would be aided by small-molecule inhibitors of O-GlcNAc transferase (OGT), the sole enzyme know to mediate this modification, but discovery of such molecules has been hampered by poor expression of cloned OGT and lack of suitable high-throughput screens. This Communication describes the

  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。
• Chemoenzymatic Synthesis of Uridine Diphosphate-GlcNAc and Uridine Diphosphate-GalNAc Analogs for the Preparation of Unnatural Glycosaminoglycans
  作者：Sayaka Masuko、Smritilekha Bera、Dixy E. Green、Michel Weïwer、Jian Liu、Paul L. DeAngelis、Robert J. Linhardt

  DOI：10.1021/jo202322k

  日期：2012.2.3

  Eight N-acetylglucosamine-1-phosphate and N-acetylgalactosamine-1-phosphate analogs have been synthesized chemically and were tested for their recognition by the GlmU uridyltransferase enzyme. Among these, only substrates that have an amide linkage to the C-2 nitrogen were transferred by GlmU to afford their corresponding uridine diphosphate(UDP)-sugar nucleotides. Resin-immobilized GlmU showed comparable activity to nonimmobilized GlmU and provides a more facile final step in the synthesis of an unnatural UDP-donor. The synthesized unnatural UDP-donors were tested for their activity as substrates for glycosyltransferases in the preparation of unnatural glycosaminoglycans in vitro. A subset of these analogs was useful as donors, increasing the synthetic repertoire for these medically important polysaccharides.
• 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.