2-acetamido-4-O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-3,6-di-O-acetyl-2-deoxy-α-D-glucopyranosyl chloride | 7531-49-9

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: 2-acetamido-4-O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-3,6-di-O-acetyl-2-deoxy-α-D-glucopyranosyl chloride
• 英文别名: βAc3GlcNAc-αAc2GlcNAc-Cl；chitobiosyl chloride；2-Acetamido-4-O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-3,6-di-O-acetyl-2-deoxy-α-D-glucopyranosylchorid；α-Acetochlorchitobiosid；GlcNAc3Ac4Ac6Ac(b1-4)a-GlcNAc1Cl3Ac6Ac；[(2R,3S,4R,5R,6S)-5-acetamido-6-[(2R,3S,4R,5R,6R)-5-acetamido-4-acetyloxy-2-(acetyloxymethyl)-6-chlorooxan-3-yl]oxy-3,4-diacetyloxyoxan-2-yl]methyl acetate
• CAS: 7531-49-9
• 化学式: C₂₆H₃₇ClN₂O₁₅
• 分子量: 653.037
• InChiKey: ZIRWPGALWMJCOT-JWVYPJMRSA-N

物化性质

• 沸点：
  796.4±60.0 °C(Predicted)
• 密度：
  1.37±0.1 g/cm3(Predicted)
• 溶解度：
  溶于氯仿

计算性质

• 辛醇/水分配系数(LogP)：
  -1.1
• 重原子数：
  44
• 可旋转键数：
  16
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.73
• 拓扑面积：
  217
• 氢给体数：
  2
• 氢受体数：
  15

反应信息

• 作为反应物：
  描述：

  2-acetamido-4-O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-3,6-di-O-acetyl-2-deoxy-α-D-glucopyranosyl chloride 在 platinum(IV) oxide 、 四(三苯基膦)钯 吗啉 、 sodium azide 、 氢气 、 甲基三辛基氯化铵 、 2-乙氧基-1-乙氧碳酰基-1,2-二氢喹啉 作用下， 以 四氢呋喃 、 二氯甲烷 、 氯仿 、 水 、 二甲基亚砜 为溶剂， 反应 76.0h， 生成 N⁴-<2-Acetamido-4-O-(2-acetamido-3,4,6-tri-O-acetyl-2-desoxy-β-D-glucopyranosyl)-3,6-di-O-acetyl-2-desoxy-β-D-glucopyranosyl>-N²-(tert-butyloxycarbonyl)-L-asparagin
  参考文献：
  名称：

  Kunz, Horst; Waldmann, Herbert; Maerz, Joachim, Liebigs Annalen der Chemie, 1989, p. 45 - 50

  摘要：

  DOI：
• 作为产物：
  描述：

  2-(乙酰氨基)-2-脱氧-4-O-[3,4,6-三-O-乙酰基-2-(乙酰氨基)-2-脱氧-beta-D-吡喃葡萄糖基]-alpha-D-吡喃葡萄糖 1,3,6-三乙酸酯 在 盐酸 、 乙酰氯 作用下， 反应 48.0h， 以82%的产率得到2-acetamido-4-O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-3,6-di-O-acetyl-2-deoxy-α-D-glucopyranosyl chloride
  参考文献：
  名称：

  （2-苯基-2-三甲基甲硅烷基）乙基-（PTMSEL）-接头在复杂细胞表面糖蛋白糖肽部分结构的合成中。

  摘要：

  （2-苯基-2-三甲基甲硅烷基）乙基-（PTMSEL）接头代表一种新型的氟化物敏感锚，用于固相合成受保护的肽和糖肽。使用二氯甲烷中的三水合四丁基氟化铵在几乎中性的条件下进行裂解，因此可以构建对碱性和酸性介质敏感的复杂分子，而碱性和酸性介质通常是裂解标准接头系统所需的。PTMSEL接头的优势在肝肠（LI）-钙粘着蛋白和粘蛋白MUC1的糖肽合成中得到了证明，这些糖肽带有碳水化合物部分，例如N-连接的壳二糖或O-连接的唾液酸-T（N）-残基。这些类型的糖肽的合成是困难的，因为它们在固相上以及在完全脱保护的形式下易于形成二级结构。使用PTMSEL接头，可以根据Fmoc策略通过自动合成来访问这些分子，而无需经常观察到副反应，例如天冬酰胺或二酮哌嗪的形成。

  DOI：

  10.1002/chem.200305304

文献信息

• Probing the mechanism of a fungal glycosyltransferase essential for cell wall biosynthesis. UDP-Chitobiose is not a substrate for chitin synthaseElectronic supplementary information (ESI) available: A. General experimental details; B. Synthesis of UDP-chitobiose (UDP-Chi); C. Procedure for chitin synthase assay; D. Data from UDP-Chi assays and E. Ki. determination. See http://www.rsc.org/suppdata/ob/b2/b208953j/
  作者：Robert Chang、Adam R. Yeager、Nathaniel S. Finney

  DOI：10.1039/b208953j

  日期：2003.12.19

  Chitin synthase is responsible for the biosynthesis of chitin, an essential component of the fungal cell wall. There is a long-standing question as to whether “processive” transferases such as chitin synthase operate in the same manner as non-processive transferases. The question arises from analysis of the polysaccharide structure – in chitin, for instance, each sugar residue is rotated ≈180° relative to the preceding sugar in the chain. This requires that the enzyme account for the alternating “up/down” configuration during biosynthesis. An enzyme with a single active site, analogous to the non-processive transferases – would have to accommodate a distorted glycosidic linkage at every other synthetic step. An alternative proposal is that the enzyme might assemble the disaccharide donor, addressing the “up/down” conformational problem prior to polymer synthesis. We present compelling evidence that this latter hypothesis is incorrect.

  几丁质合酶负责几丁质的生物合成，几丁质是真菌细胞壁的基本成分。长期以来有一个问题是：“机动性”转移酶（如几丁质合酶）是否以与非机动性转移酶相同的方式工作。这一问题源于多糖结构的分析——例如在几丁质中，每一糖残基相对于链中前面的糖残基旋转约180度。这就要求该酶在生物合成过程中考虑“上/下”交替的构型。与非机动性转移酶类似，具有单个活性部位的酶必须在每第二次合成步骤中适应扭曲的糖苷键。另一个提案是酶可能在聚合物合成之前组装二糖供体，解决“上/下”构象问题。我们提供了令人信服的证据，表明这后一种假设是不正确的。
• WO2008/153394
  申请人：——

  公开号：——

  公开（公告）日：——
• Thiem, Joachim; Wiemann, Torsten, Angewandte Chemie, 1990, vol. 102, # 1, p. 78 - 80
  作者：Thiem, Joachim、Wiemann, Torsten

  DOI：——

  日期：——
• Substrate Specificity of the Glycosyl Donor for Oligosaccharyl Transferase
  作者：Vincent W.-F. Tai、Barbara Imperiali

  DOI：10.1021/jo0100345

  日期：2001.9.1

  Oligosaccharyl transferase (OT) catalyzes the co-translational transfer of a dolichol-linked tetradecasaccharide (Dol-PP-GlcNAc(2)Man(9)Glc(3),1a) to an asparagine side chain of a nascent polypeptide inside the lumen of the endoplasmic reticulum. (ER). The glycosyl acceptor requires an Asn-Xaa-Thr/Ser sequon, where Xaa can be any natural amino acid except proline, for N-linked glycosylation to occur. To address the substrate specificity of the glycosyl donor, three unnatural dolichol-linked disaccharide analogues (Dol-PP-GlcNTFA-GlcNAc 1c, Dol-PP-2DFGlc-GlcNAc Id, and Dol-PP-GlcNAc-Glc le) were synthesized and evaluated as substrates or inhibitors for OT from yeast. The synthetic analogue Dol-PP-GlcNAc-Glc le, with substitution in the distal sugar, was found to be a substrate (K-mapp = 26 muM for OT. On the other hand, the analogues Dol-PP-GlcNTFA-GlcNAc le (Ki = 154 muM) and Dol-PP-2DFGlc-GlcNAc 1d (K-i = 25 muM), with variations in the proximal sugar, were inhibitors for OT. The dolichol-linked monosaccharide Dol-PP-GlcNAc 3 was found to be the minimum unit for glycosylation to occur.
• Enzyme-catalyzed glycosylation of peptides using a synthetic lipid disaccharide substrate
  作者：Jung Lee、James K. Coward

  DOI：10.1021/jo00041a015

  日期：1992.7

  A lipid disaccharide, consisting of chitobiose linked to dilichol via an alpha-1-pyrophosphate, has been synthesized for use as a substrate in the enzyme-catalyzed glycosylation of peptides. For the purpose of confirming the structure of the reaction product, the expected glycopeptide was synthesized via an unambiguous, convergent method. Chromatographic and spectral comparison of the synthetic vs biosynthetic glycopeptides showed that they were identical. Thus, glycosylation of synthetic peptides by a synthetically accessible lipid disaccharide can be effected using oligosaccharyltransferase isolated from yeast.