(3-aminopropyl)-β-D-galactopyranosyl-(1→3)-2-acetamido-2-deoxy-β-D-glucopyranoside | 75598-07-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (3-aminopropyl)-β-D-galactopyranosyl-(1→3)-2-acetamido-2-deoxy-β-D-glucopyranoside
• 英文别名: β-D-galactopyranosyl-(1–3)-2-acetamido-2-deoxy-D-glucopyranose；lacto-N-biose I；βDGal(1-3)βDGlcNAc；2-acetamido-2-deoxy-3-O-beta-D-galactopyranosyl-beta-D-glucopyranose；N-[(2R,3R,4R,5S,6R)-2,5-dihydroxy-6-(hydroxymethyl)-4-[(2R,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-3-yl]acetamide
• CAS: 75598-07-1
• 化学式: C₁₄H₂₅NO₁₁
• 分子量: 383.353
• InChiKey: HMQPEDMEOBLSQB-LODBTCKLSA-N

物化性质

• 熔点：
  168-169 °C
• 沸点：
  795.5±60.0 °C(Predicted)
• 密度：
  1?+-.0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -4.2
• 重原子数：
  26
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.93
• 拓扑面积：
  198
• 氢给体数：
  8
• 氢受体数：
  11

反应信息

• 作为反应物：
  描述：

  (3-aminopropyl)-β-D-galactopyranosyl-(1→3)-2-acetamido-2-deoxy-β-D-glucopyranoside 、 5`-二磷酸鸟嘌呤核苷-岩藻糖二钠盐 在 ammonium hydroxide 作用下， 以 水 、 异丙醇 为溶剂， 生成 Fuc(b1-2)Gal(b1-3)b-GlcNAc
  参考文献：
  名称：

  Biochemical characterization of an α1,2-colitosyltransferase fromEscherichia coliO55:H7

  摘要：

  Colitose，也称为 3,6-二脱氧-L-半乳糖或 3-脱氧-L-岩藻糖，是仅有的五种天然存在的 3,6-二脱氧己糖之一。在许多感染性细菌的脂多糖中发现了大肠糖，包括大肠杆菌 O55 和 O111 以及霍乱弧菌 O22 和 O139。迄今为止，尚未对大肠糖基转移酶 (ColT) 进行表征，这可能是由于糖供体 GDP-大肠糖难以获得。在本研究中，从化学制备的大肠糖开始，通过简便高效的一锅双酶系统制备了 94.6 毫克 GDP-大肠糖，该系统涉及 l-岩藻糖激酶/GDP-l-Fuc 焦磷酸化酶和无机焦磷酸酶 (EcPpA)。 WbgN（一种来自大肠杆菌 O55:H5 的假定 ColT）随后通过使用 GDP-colitose 作为糖供体进行克隆、过表达、纯化和生化表征。合成产物的活性测定和结构鉴定清楚地表明 wbgN 编码 α1,2-ColT。生物物理研究表明WbgN不需要金属离子，并且在pH 7.5-9.0时具有高活性。此外，受体特异性研究表明，WbgN 专门识别乳-N-二糖 (Galβ1,3-GlcNAc)。最有趣的是，我们发现 WbgN 对 GDP-l-Fuc (kcat/Km = 9.2 min−1 mM−1) 的活性与对 GDP-colitose (kcat/Km = 12 min−1 mM−1) 的活性相似。最后，利用这一点，成功地制备级合成了1型H抗原。

  DOI：

  10.1093/glycob/cwv169
• 作为产物：
  描述：

  在 sodium hydroxide 作用下， 以 水 为溶剂， 反应 7.0h， 以96%的产率得到(3-aminopropyl)-β-D-galactopyranosyl-(1→3)-2-acetamido-2-deoxy-β-D-glucopyranoside
  参考文献：
  名称：

  The synthesis of oligosaccharides containing internal and terminal Galβ1-3GlcNAcβ fragments

  摘要：

  Oligosaccharides Gal beta 1-3GlcNAc beta-sp, GlcNAc beta 1-3Gal beta 1-3GlcNAc beta-sp, Gal beta 1-3GlcNAc beta 1-3Gal beta 1-3GlcNAc beta-sp, Gal beta 1-3GlcNAc beta 1-3Gal beta 1-4GlcNAc beta-sp, Gal beta 1-3GlcNAc beta 1-6Gal beta 1-4GlcNAc beta-sp (sp = O(CH2)(3)NH2 or O(CH2)(2)NH2) were synthesized using glycosylation with N-Troc-protected derivatives of glucosamine or disaccharide Le(c).

  DOI：

  10.1134/s1068162015020120

文献信息

• The characterisation of a galactokinase from Streptomyces coelicolor
  作者：Tessa Keenan、Rhys Mills、Emily Pocock、Darshita Budhadev、Fabio Parmeggiani、Sabine Flitsch、Martin Fascione

  DOI：10.1016/j.carres.2018.12.005

  日期：2019.1

  Promiscuous galactokinases (GalKs), which catalyse the ATP dependent phosphorylation of galactose in nature, have been widely exploited in biotechnology for the rapid synthesis of diverse sugar-1-phosphates. This work focuses on the characterisation of a bacterial GalK from Streptomyces coelicolor (ScGalK), which was overproduced in Escherichia coli and shown to phosphorylate galactose. ScGalK displayed

  混杂半乳糖激酶（GalKs）催化自然界中半乳糖的ATP依赖性磷酸化，已在生物技术中得到广泛利用，以快速合成各种糖-1-磷酸。这项工作的重点是表征一种来自Coelicolor链霉菌（ScGalK）的细菌GalK的特性，该细菌在大肠杆菌中过量生产，并且可以磷酸化半乳糖。ScGalK具有广泛的底物耐受性，对Gal，GalN，Gal3D，GalNAc，Man和L-Ara具有活性。最有趣的是，ScGalK在很宽的pH和温度范围内显示出高活性，表明该酶可能高度适合多酶系统。
• Modified sialyl Lewis.sup.a compounds
  申请人：Alberta Research Council

  公开号：US05872096A1

  公开（公告）日：1999-02-16

  The present invention is drawn to methods for the synthesis of Lewis.sup.a derivatives modified at the C-2 and/or C-6 position of GlcNAc employing chemo-enzymatic synthesis. The derivatives find use in the treatment and prevention of diseases.

  本发明涉及使用化学酶合成的方法合成在GlcNAc的C-2和/或C-6位置修饰的Lewis.sup.a衍生物。这些衍生物可用于治疗和预防疾病。
• Modified sialyl Lewis.sup.x compounds
  申请人：Alberta Research Council

  公开号：US05939290A1

  公开（公告）日：1999-08-17

  The present invention is drawn to methods for the synthesis of sialyl Lewis.sup.x derivatives modified at the C-2 and/or C-6 position of GlcNAc employing chemoenzymatic synthesis. The derivatives find use in the treatment and prevention of diseases.

  本发明涉及使用化学酶合成方法合成在GlcNAc的C-2和/或C-6位置修饰的唾液酸Lewis.sup.x衍生物的方法。这些衍生物可用于治疗和预防疾病。
• A combined chemical and enzymatic strategy for the construction of carbohydrate-containing antigen core units
  作者：Gary C. Look、Yoshitaka Ichikawa、Gwo Jenn Shen、Pi Wan Cheng、Chi Huey Wong

  DOI：10.1021/jo00068a030

  日期：1993.7

  Glycosidase-mediated coupling of glycal acceptors with galactose donors affords beta1,3-linked disaccharides that are versatile intermediates for further chemical and enzymatic manipulation. The utility of these disaccharides is demonstrated by the elaboration of these compounds into the type I and type IV core disaccharides of carbohydrate-containing antigens. Further conversion of the type IV disaccharide to a mucin-type trisaccharide (Galbeta1,3(GlcNAcbeta1,6)GalNAc) was accomplished with the use of a beta1,6-N-acetylglucosaminyltransferase. This combined use of enzymatic and chemical methodologies allows for the rapid assembly, with high regio- and stereoselectivity, of core oligosaccharides of biologically important glycoconjugates.
• Crystal Structures of a Glycoside Hydrolase Family 20 Lacto-N-biosidase from Bifidobacterium bifidum
  作者：Tasuku Ito、Takane Katayama、Mitchell Hattie、Haruko Sakurama、Jun Wada、Ryuichiro Suzuki、Hisashi Ashida、Takayoshi Wakagi、Kenji Yamamoto、Keith A. Stubbs、Shinya Fushinobu

  DOI：10.1074/jbc.m112.420109

  日期：2013.4

  Human milk oligosaccharides contain a large variety of oligosaccharides, of which lacto-N-biose I (Gal-beta 1,3-GlcNAc; LNB) predominates as a major core structure. A unique metabolic pathway specific for LNB has recently been identified in the human commensal bifidobacteria. Several strains of infant gut-associated bifidobacteria possess lacto-N-biosidase, a membrane-anchored extracellular enzyme, that liberates LNB from the nonreducing end of human milk oligosaccharides and plays a key role in the metabolic pathway of these compounds. Lacto-N-biosidase belongs to the glycoside hydrolase family 20, and its reaction proceeds via a substrate-assisted catalytic mechanism. Several crystal structures of GH20 beta-N-acetylhexosaminidases, which release monosaccharide GlcNAc from its substrate, have been determined, but to date, a structure of lacto-N-biosidase is unknown. Here, we have determined the first three-dimensional structures of lacto-N-biosidase from Bifidobacterium bifidum JCM1254 in complex with LNB and LNB-thiazoline (Gal-beta 1,3-GlcNAc-thiazoline) at 1.8-angstrom resolution. Lacto-N-biosidase consists of three domains, and the C-terminal domain has a unique beta-trefoil-like fold. Compared with other beta-N-acetylhexosaminidases, lacto-N-biosidase has a wide substrate-binding pocket with a -2 subsite specific for beta-1,3-linked Gal, and the residues responsible for Gal recognition were identified. The bound ligands are recognized by extensive hydrogen bonds at all of their hydroxyls consistent with the enzyme's strict substrate specificity for the LNB moiety. The GlcNAc sugar ring of LNB is in a distorted conformation near E-4, whereas that of LNB-thiazoline is in a C-4(1) conformation. A possible conformational pathway for the lacto-N-biosidase reaction is discussed.