| 1067638-67-8

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷酸
• CAS: 1067638-67-8
• 化学式: C₁₈H₂₈N₆O₁₄P₂
• 分子量: 614.4
• InChiKey: HYGUPIQCOQWMBA-MDBFFHOUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.75
• 重原子数：
  40.0
• 可旋转键数：
  10.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  300.39
• 氢给体数：
  8.0
• 氢受体数：
  17.0

反应信息

• 作为产物：
  描述：

  [(2R,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl] dihydrogen phosphate;azane 、 2'-脱氧腺苷 5'-三磷酸酯 在 sodium chloride 、 magnesium chloride 作用下， 以 aq. buffer 为溶剂， 反应 0.5h， 以6.47%的产率得到
  参考文献：
  名称：

  Probing the roles of conserved residues in uridyltransferase domain of Escherichia coli K12 GlmU by site-directed mutagenesis

  摘要：

  N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme that catalyzes both acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthesis pathway. Our previous study demonstrated that the uridyltransferase domain of GlmU (tGlmU) exhibited a flexible substrate specificity, which could be further applied in unnatural sugar nucleotides preparation. However, the structural basis of tolerating variant substrates is still not clear. Herein, we further investigated the roles of several highly conserved amino acid residues involved in substrate binding and recognition by structure-and sequence-guided site-directed mutagenesis. Out of total 16 mutants designed, tGlmU Q76E mutant which had a novel catalytic activity to convert CTP and GlcNAc-1P into unnatural sugar nucleotide CDP-GlcNAc was identified. Furthermore, tGlmU Y103F and N169R mutants were also investigated to have enhanced uridyltransferase activities compared with wide-type tGlmU. (C) 2015 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2015.05.007

文献信息

• Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12
  作者：Junqiang Fang、Wanyi Guan、Li Cai、Guofeng Gu、Xianwei Liu、Peng George Wang

  DOI：10.1016/j.bmcl.2009.09.039

  日期：2009.11

  N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Escherichia coli K12 is a bifunctional enzyme that catalyzes both the acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthetic pathway. In this study, we report the broad substrate specificity of the pyrophosphorylase domain of GlmU during its uridyltransfer reaction and the substrate priority is ranked in the following order: UTP > dUTP > dTTP >> CTP > dATP/dm(6) ATP. This pyrophosphorylase domain of GlmU is also a tool to synthesize UDP-GlcNAc analogs, two examples of which were synthesized herein in multiple mg scale in vitro. (C) 2009 Elsevier Ltd. All rights reserved.