3,4,6-tri-O-acetyl-2-acetamido-2-deoxy-α-D-galactopyranosyl dihydrogen phosphate | 92283-18-6

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 3,4,6-tri-O-acetyl-2-acetamido-2-deoxy-α-D-galactopyranosyl dihydrogen phosphate
• 英文别名: N-acetylgalactosamine-1-phosphate；2-Acetamido-2-desoxy-D-galactopyranose-α-1-phosphat；N-Acetyl-alpha-D-galactosamine 1-phosphate；[(2R,3R,4R,5R,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl] dihydrogen phosphate
• CAS: 92283-18-6
• 化学式: C₈H₁₆NO₉P
• 分子量: 301.19
• InChiKey: FZLJPEPAYPUMMR-JAJWTYFOSA-N

物化性质

• 密度：
  1.70±0.1 g/cm3(Predicted)
• 物理描述：
  Solid

计算性质

• 辛醇/水分配系数(LogP)：
  -3.7
• 重原子数：
  19
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  166
• 氢给体数：
  6
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  3,4,6-tri-O-acetyl-2-acetamido-2-deoxy-α-D-galactopyranosyl dihydrogen phosphate 、 尿苷-5'-三磷酸 在 yeast inorganic pyrophosphatase 、 N-acetylglucosamine-1-phosphate pyrophosphorylase from C_. jejuni NCTC 11168 、 三羟甲基氨基甲烷盐酸盐 、 magnesium chloride 作用下， 反应 2.0h， 以12.7%的产率得到uridine-5'-diphospho-N-acetyl-D-galactosamine
  参考文献：
  名称：

  A chemoenzymatic route to synthesize unnatural sugar nucleotides using a novel N-acetylglucosamine-1-phosphate pyrophosphorylase from Camphylobacter jejuni NCTC 11168

  摘要：

  A novel N-acetylglucosamine-1-phosphate pyrophosphorylase was identified from Campylobacter jejuni NCTC 11168. An unprecedented degree of substrate promiscuity has been revealed by systematic studies on its substrate specificities towards sugar-1-P and NTP. The yields of the synthetic reaction of seven kinds of sugar nucleotides catalyzed by the enzyme were up to 60%. In addition, the yields of the other nine were around 20%. With this enzyme, three novel sugar nucleotide analogs were synthesized on a preparative scale and well characterized. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.06.003
• 作为产物：
  描述：

  α-D-galactosamine 1-phosphate 、 S-acetyl coenzyme A 在 Pyrococcus furiosus enzyme 、 magnesium 作用下， 以 various solvent(s) 为溶剂， 反应 0.67h， 生成 3,4,6-tri-O-acetyl-2-acetamido-2-deoxy-α-D-galactopyranosyl dihydrogen phosphate
  参考文献：
  名称：

  One-Step Synthesis of Labeled Sugar Nucleotides for Protein O-GlcNAc Modification Studies by Chemical Function Analysis of an Archaeal Protein

  摘要：

  Herein we present the chemical function analysis of a recombinant sugar nucleotidyltransferase from the hyperthermophile Pyrococcus furiosus and its use in the one-pot synthesis of chloroacetyl- and alkyne-tagged analogues of uridinediphospho-N-acetylglucosamine (UDP-GlcNAc). The gene was originally annotated as a glucose-1-phosphate deoxythymidylyltransferase; however, kinetic analysis of a panel of sugar-1-phosphates with the protein shows that it is better described as a bifunctional protein that synthesizes UDP-GlcNAc from glucosamine-1-phosphate and acetyl coenzyme A (CoA). A new mass-spectrometry-based assay for the rapid analysis of the acyltransferase activity demonstrates that the enzyme can also accept cheaper truncated N-acetylcysteamine thioester substrates in place of the natural acetyl CoA. The enzyme can tolerate alkyne or chloride substitutions in the acyl moiety, thereby allowing the facile synthesis of tagged sugar nucleotides for future use in protein O-GlcNAc modification studies.

  DOI：

  10.1021/ja044117p

文献信息

• Wide sugar substrate specificity of galactokinase from Streptococcus pneumoniae TIGR4
  作者：Min Chen、Lei-lei Chen、Yang Zou、Mengyang Xue、Min Liang、Lan Jin、Wan-yi Guan、Jie Shen、Wenjun Wang、Lei Wang、Jun Liu、Peng George Wang

  DOI：10.1016/j.carres.2011.08.014

  日期：2011.11

  Galactokinases (GALK) have attracted significant research attention for their potential application in the enzymatic synthesis of unique sugar phosphates. The galactokinase (GalKSpe4) cloned from Streptococcus pneumoniae TIGR4 had a temperature optimum of 45 C, and a pH optimum of 8.0. The substrate specificity and kinetics studies revealed that GalKSpe4 had moderate activity toward glucose, in contrast with very low or no activity observed in other previously reported GALKs. Most interestingly, GalKSpe4 exhibited activity for GalNAc, which had never been recorded in other GALKs found by now. This is the first time to report that bacterial GALK can recognize GalNAc. (C) 2011 Published by Elsevier Ltd.
• Synthesis of a fluorescent acceptor substrate for glycosyltransferases involved in the assembly of O-antigens of enterohemorrhagic Escherichia coli O157 and O5
  作者：Anna N. Vinnikova、Tatyana N. Druzhinina、Leonid L. Danilov、Natalia S. Utkina、Vladimir I. Torgov、Vladimir V. Veselovsky、Shuo Wang、Bin Liu、Lei Wang、Inka Brockhausen

  DOI：10.1016/j.carres.2012.11.009

  日期：2013.1

  The assembly of the repeating units of O-antigens in Gram negative bacteria is catalyzed by specific glycosyltransferases. Previously we used GlcNAc/GalNAc alpha-diphosphate-phenoxyundecyl as natural acceptor substrate analogs in assays of the transfer of radioactive sugars by bacterial glycosyltransferases. In order to develop new, fluorescence based assays we have synthesized a fluorescent acceptor P-1-[11-(anthracen-9-ylmethoxy)undecyl]-P-2-(2-acetamido-2-deoxy-alpha-D-galactopyranosyl) diphosphate and have shown that the compound was an excellent acceptor for glucosyltransferase WbdN from Escherichia coli (E. coli) O157 and for galactosyltransferase WbwC from E. coli O5. This is the first report of the Galtransferase activity of the wbwC gene product of E. coli O5. The presence of the fluorescent label in the acceptor molecule allows the detection of glycosyltransferase reaction products with high sensitivity, eliminating the need for radioactive nucleotide sugars. (C) 2012 Elsevier Ltd. All rights reserved.
• [EN] ACHOLETIN BIOPOLYMERS AND METHODS FOR ENZYMATIC SYNTHESIS<br/>[FR] BIOPOLYMÈRES D'ACHOLÉTINE ET PROCÉDÉS DE SYNTHÈSE ENZYMATIQUE
  申请人：[en]THE UNIVERSITY OF BRITISH COLUMBIA

  公开号：WO2022256920A1

  公开（公告）日：2022-12-15

  Provided herein are β-1,3-linked biopolymers (acholetin polysaccharides). Furthermore, provided herein are enzymatic methods and systems for producing β-1,3-linked oligosaccharides and polysaccharides using β-1,3-N-acetylglucosaminide phosphorylase (Acholetin phosphorylase (AchP)). The AchP was sourced from the genome of the cell wall-less Mollicute bacterium, Acholeplasma laidlawii and was found to synthesize β-1,3-linked N-acetylglucosamine (GlcNAc) or N-acetylgalactosamine (GalNAc) oligomers using the donor, α-N-acetylglucosamine 1-phosphate (GlcNAc1-P) or N-acetylgalactosamine 1-phosphate (GalNAc1-P).