dTDP-6-deoxy-L-talose

• 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: dTDP-6-deoxy-L-talose
• 英文别名: dTDP-6dTal；dTDP-6-deoxy-beta-L-talose(2-)；[[(2R,3S,5R)-3-hydroxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-oxidophosphoryl] [(2R,3R,4R,5S,6S)-3,4,5-trihydroxy-6-methyloxan-2-yl] phosphate
• 化学式: C₁₆H₂₄N₂O₁₅P₂
• 分子量: 546.318
• InChiKey: ZOSQFDVXNQFKBY-ONRKHWABSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  -5.2
• 重原子数：
  35
• 可旋转键数：
  8
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  257
• 氢给体数：
  5
• 氢受体数：
  15

反应信息

• 作为反应物：
  描述：

  dTDP-6-deoxy-L-talose 生成 dTDP-β-L-Rha
  参考文献：
  名称：

  A new route to dTDP-6-deoxy- l -talose and dTDP- l -rhamnose: dTDP- l -rhamnose 4-epimerase in Burkholderia thailandensis

  摘要：

  dTDP-L-rhamnose (dTDP-Rha)-synthesizing dTDP-6-deoxy-L-lyxo-4-hexulose reductase (4-KR) and dTDP-Rha 4-epimerase were characterized from Burkholderia thailandensis E264 by utilizing rmlD(Bth) (BTH_I1472) and wbiB(Bth) (BTH_I1476), respectively. Incubation of the recombinant WbiB(Bth) with RmlA/RmlB/RmlC/Tal, which has previously been shown to generate dTDP-6-deoxy-L-talose (dTDP-6dTal) from alpha-D-glucose-1-phosphate, dTTP, and NADPH, produced dTDP-Rha. H-1 NMR measurements confirmed that both RmlA/RmlB/RmlC/Tal/WbiB(Bth) and RmlA/RmlB/RmlC/RmlD produced dTDP-Rha. WbiB(Bth) alone produced dTDP-Rha when incubated with dTDP-6dTal. This is the first report to demonstrate epimerase activity interconverting between dTDP-Rha and dTDP-6dTal. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.05.030
• 作为产物：
  描述：

  胸苷-5'-三磷酸 、 对氟苯甲醇 在 potassium dihydrogenphosphate 、 pyrophosphatase 、 Kitasatospora kifunensis MJM₃₄₁ recombinant RmlA protein 、 Kitasatospora kifunensis MJM₃₄₁ recombinant RmlB protein 、 magnesium chloride 、 Kitasatospora kifunensis MJM₃₄₁ recombinant RmlC protein 、 Kitasatospora kifunensis MJM₃₄₁ recombinant Tal protein 、 β-烟酰胺腺嘌呤二核苷酸 作用下， 以 水 为溶剂， 反应 2.0h， 生成 dTDP-4-keto-6-deoxy-D-glucose 、 dTDP-D-glucose 、 dTDP-6-deoxy-L-talose
  参考文献：
  名称：

  Cloning and in vitro characterization of dTDP-6-deoxy-l-talose biosynthetic genes from Kitasatospora kifunensis featuring the dTDP-6-deoxy-l-lyxo-4-hexulose reductase that synthesizes dTDP-6-deoxy-l-talose

  摘要：

  Kitasatospora kifunensis, the talosin producer, was used as a source for the dTDP-6-deoxy-L-talose (dTDP-6dTal) biosynthetic gene cluster, serving as a template for four recombinant proteins of RmlA(Kkf), RmlB(Kkf), RmlC(Kkf), and Tal, which complete the biosynthesis of dTDP-6dTal from dTTP, alpha-D-glucose-1-phosphate, and NAD(P)H. The identity of dTDP-6dTal was validated using H-1 and C-13 NMR spectroscopy. K. kifunensis tal and tll, the known dTDP-6dTal synthase gene of Actinobacillus actinomycetemcomitans origin, have low sequence similarity and are distantly related within the NDP-6-deoxy-4-ketohexose reductase family, providing an example of the genetic diversity within the dTDP-6dTal biosynthetic pathway. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2010.07.004

文献信息

• Gaugler R.W.; Gabriel O., J Biol Chem, 1973, 0021-9258, 6041-9
  作者：Gaugler R.W.、Gabriel O.

  DOI：——

  日期：——
• Thymidine Diphosphate-6-deoxy-l-lyxo-4-hexulose Reductase Synthesizing dTDP-6-deoxy-l-talose fromActinobacillus actinomycetemcomitans
  作者：Yoshio Nakano、Nao Suzuki、Yasuo Yoshida、Takashi Nezu、Yoshihisa Yamashita、Toshihiko Koga

  DOI：10.1074/jbc.275.10.6806

  日期：2000.3

  The serotype c-specific polysaccharide antigen of Actinobacillus actinomycetemcomitans NCTC 9710 contains an unusual sugar, 6-deoxy-L-talose, which has been identified as a constituent of cell wall components in some bacteria. Two genes coding for thymidine diphosphate (dTDP)-6-deoxy-L-lyxo-4-hexulose reductases were identified in the gene cluster required for biosynthesis of serotype c-specific polysaccharide. Both dTDP-6-deoxy-L-lyxo-4-hexulose reductases were overproduced and purified from Escherichia coli transformed with the plasmids containing these genes. The sugar nucleotides converted by both reductases were purified by reversed-phase high performance liquid chromatography and identified by III nuclear magnetic resonance and gas-liquid chromatography. The results indicated that one of two reductases produced dTDP-6-deoxy-L-talose and the other produced dTDP-L-rhamnose (dTDP-6-deoxy-L-mannose). The amino acid sequence of the dTDP-6-deoxy-L-oxy-L-lyxo-4-hexulose reductase forming dTDP-6-deoxy-L-talose shared only weak homology with that forming dTDP-L-rhamnose, despite the fact that these two enzymes catalyze the reduction of the same substrate and the products are determined by the stereospecificity of the reductase activity. Neither the gene for dTDP-6-deoxy-L-talose biosynthesis nor its corresponding protein product has been found in other bacteria; this biosynthetic pathway is identified here for the first time.