UDP-6dGlc

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘧啶核苷酸
• 英文名称: UDP-6dGlc
• 英文别名: Uridine 5'-diphospo-6-deoxy-alpha-D-glucopyranoside；[[(2R,3S,4R,5R)-5-(2,4-dioxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-oxidophosphoryl] [(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-methyloxan-2-yl] phosphate
• 化学式: C₁₅H₂₂N₂O₁₆P₂
• 分子量: 548.291
• InChiKey: DRDCJEIZVLVWNC-JZMIEXBBSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  -6
• 重原子数：
  35
• 可旋转键数：
  8
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.73
• 拓扑面积：
  277
• 氢给体数：
  6
• 氢受体数：
  16

反应信息

• 作为产物：
  描述：

  6dGlc-1-phosphate 、 尿苷-5'-三磷酸 在 magnesium Escherichia coli UDP-glucose pyrophosphorylase 、 inorganic pyrophosphorylase 、 三羟甲基氨基甲烷 作用下， 以 水 为溶剂， 反应 0.08h， 生成 UDP-6dGlc
  参考文献：
  名称：

  Strategies for the Chemoenzymatic Synthesis of Deoxysugar Nucleotides:  Substrate Binding versus Catalysis

  摘要：

  Sugar nucleotidyltransferases, also known as sugar pyrophosphorylases, catalyze the formation of a phosphate linkage to produce sugars activated for use by Leloir pathway glycosyltransferases and are subjects of protein engineering for chemoenzymatic synthesis strategies. Herein we present evidence that differences in substrate binding affinity do not primarily account for substantial contrasts in deoxysugar nucleotide product yields with this class of enzymes. Prokaryotic and eukaryotic glucose-1-phosphate uridylyltransferases (EC 2.7.7.9) can exercise kinetic discrimination in choosing carbohydrates of comparable binding affinity for catalytic turnover. These findings have implications for the in vivo and in vitro function and use of these enzymes.

  DOI：

  10.1021/jo048424p

文献信息

• Strategies for the Chemoenzymatic Synthesis of Deoxysugar Nucleotides:  Substrate Binding versus Catalysis
  作者：Kwang-Seuk Ko、Corbin J. Zea、Nicola L. Pohl

  DOI：10.1021/jo048424p

  日期：2005.3.1

  Sugar nucleotidyltransferases, also known as sugar pyrophosphorylases, catalyze the formation of a phosphate linkage to produce sugars activated for use by Leloir pathway glycosyltransferases and are subjects of protein engineering for chemoenzymatic synthesis strategies. Herein we present evidence that differences in substrate binding affinity do not primarily account for substantial contrasts in deoxysugar nucleotide product yields with this class of enzymes. Prokaryotic and eukaryotic glucose-1-phosphate uridylyltransferases (EC 2.7.7.9) can exercise kinetic discrimination in choosing carbohydrates of comparable binding affinity for catalytic turnover. These findings have implications for the in vivo and in vitro function and use of these enzymes.