[(2R,3R,4S,5S,6S)-5-amino-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl] dihydrogen phosphate | 345197-23-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: [(2R,3R,4S,5S,6S)-5-amino-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl] dihydrogen phosphate
• CAS: 345197-23-1
• 化学式: C₆H₁₄NO₈P
• 分子量: 259.153
• InChiKey: JCTUIUVCJUPPPW-VFUOTHLCSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -6.2
• 重原子数：
  16
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  163
• 氢给体数：
  6
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  [(2R,3R,4S,5S,6S)-5-amino-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl] dihydrogen phosphate 、 胸苷-5'-三磷酸 在 无机焦磷酸酶 、 RmlA-L₈₉T 、 magnesium chloride 作用下， 反应 3.0h， 生成 2'-Deoxythymidine-5'-diphospho-(4''-amino-4''-deoxy-α-D-glucopyranose)
  参考文献：
  名称：

  Characterization of CalE10, the N-Oxidase Involved in Calicheamicin Hydroxyaminosugar Formation

  摘要：

  As the first in vitro characterization of a sugar N-oxidase, this study establishes CalE10 as the key oxidase involved in calicheamicin hydroxylamino glycoside formation. This Study confirms that oxidation occurs at the sugar nucleotide stage prior to glycosyltransfer, and substrate specificity studies reveal CalE10-catalyzed oxidation to be regiospecific and to present trace amounts of the corresponding nitrosugar in vitro. This work also sets a precedent for the future study of other N-oxidases involved in hydroxylamino-, nitroso-, and/or nitrosugar formation.

  DOI：

  10.1021/ja807557a

文献信息

• Characterization of CalE10, the <i>N</i>-Oxidase Involved in Calicheamicin Hydroxyaminosugar Formation
  作者：Heather D. Johnson、Jon S. Thorson

  DOI：10.1021/ja807557a

  日期：2008.12.31

  As the first in vitro characterization of a sugar N-oxidase, this study establishes CalE10 as the key oxidase involved in calicheamicin hydroxylamino glycoside formation. This Study confirms that oxidation occurs at the sugar nucleotide stage prior to glycosyltransfer, and substrate specificity studies reveal CalE10-catalyzed oxidation to be regiospecific and to present trace amounts of the corresponding nitrosugar in vitro. This work also sets a precedent for the future study of other N-oxidases involved in hydroxylamino-, nitroso-, and/or nitrosugar formation.