2-脱氧核糖5-磷酸酯 | 7685-50-9

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机磷酸及其衍生物
• 中文名称: 2-脱氧核糖5-磷酸酯
• 英文名称: 2-deoxy-D-ribose 5-phosphate
• 英文别名: 2-deoxy-5-O-phosphono-D-erythro-pentose；[(2R,3S)-2,3-dihydroxy-5-oxopentyl] dihydrogen phosphate
• CAS: 7685-50-9
• 化学式: C₅H₁₁O₇P
• 分子量: 214.112
• InChiKey: ALQNUOMIEBHXQG-CRCLSJGQSA-N

物化性质

• 沸点：
  541.3±60.0 °C(Predicted)
• 密度：
  1.651±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -3.4
• 重原子数：
  13
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.8
• 拓扑面积：
  124
• 氢给体数：
  4
• 氢受体数：
  7

安全信息

• 海关编码：
  2919900090

反应信息

• 作为反应物：
  描述：

  2-脱氧核糖5-磷酸酯 、 磷烯醇丙酮酸 在 DAH 7-P synthase 、 Tris buffer 、 manganese(ll) chloride 作用下， 以 水 为溶剂， 反应 0.17h， 以94%的产率得到(2R,4S,6S)-2,4-dihydroxy-6-[(1R)-1-hydroxy-2-phosphonooxyethyl]oxane-2-carboxylic acid
  参考文献：
  名称：

  Enzymatic Synthesis of 3-Deoxy-d-manno-octulosonate 8-Phosphate, 3-Deoxy-d-altro-octulosonate 8-Phosphate, 3,5-Dideoxy-d-gluco(manno)-octulosonate 8-Phosphate by 3-Deoxy-d-arabino-heptulosonate 7-Phosphate Synthase

  摘要：

  The phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH 7-P) synthase (phe), a key enzyme involved in the biosynthesis of the aromatic amino acid phenylalanine, expressed by the Escherichia coli gene aroG, which catalyzes the condensation of D-erythrose 4-phosphate with phosphoenolpyruvate (PEP) to give DAH 7-P, was cloned into the expression vector pT7-7 for overexpression in E. coli. Purified enzyme from this expression system was used to demonstrate that DAH 7-P synthase (phe) also catalyses the aldol-type condensation of PEP with the 5-carbon analogues D-arabinose 5-phosphate, D-ribose 5-phosphate, and 2-deoxy-D-ribose 5-phosphate to yield 3-deoxy-D-manno-octulosonate 8-phosphate, 3-deoxy-D-altro-octulosonate 8-phosphate, and 3,5-dideoxy-D-gluco(manno)-octulosonate 8-phosphate, respectively, as determined by H-1 NMR and other standard analytical methods. The kinetic parameters, K-m and V-max, for these reactions were determined. The 3- and 6-carbon phosphorylated monosaccharides, D,L-glyceraldehyde 3-phosphate and D-glucose 6-phosphate, as well as the nonphosphorylated 5-carbon analogues D-arabinose 5-phosphate, D-ribose 5-phosphate, and 2-deoxy-D-ribose 5-phosphate were not substrates.

  DOI：

  10.1021/ja9816281
• 作为产物：
  描述：

  果糖二磷酸钠 在 deoxyriboaldolase-substances 、 muscle aldolase-substances 、 乙醛 作用下， 生成 2-脱氧核糖5-磷酸酯
  参考文献：
  名称：

  Racker, Journal of Biological Chemistry, 1952, vol. 196, p. 347,359

  摘要：

  DOI：

文献信息

• Structure-Based mutagenesis approaches toward expanding the substrate specificity of d-2-Deoxyribose-5-phosphate aldolase
  作者：Grace DeSantis、Junjie Liu、David P Clark、Andreas Heine、Ian A Wilson、Chi-Huey Wong

  DOI：10.1016/s0968-0896(02)00429-7

  日期：2003.1

  2-Deoxyribose-5-phosphate aldolase (DERA, EC 4.1.2.4) catalyzes the reversible aldol reaction between acetaldehyde and D-glyceraldehyde-3-phosphate to generate D-2-deoxyribose-5-phosphate. It is unique among the aldolases as it catalyzes the reversible asymmetric aldol addition reaction of two aldehydes. In order to expand the substrate scope and stereoselectivity of DERA, structure-based substrate design as well

  2-脱氧核糖5-磷酸醛缩酶（DERA，EC 4.1.2.4）催化乙醛和D-甘油醛-3-磷酸之间的可逆醛醇缩合反应，生成D-2-脱氧核糖-5-磷酸。它在醛缩酶中是独特的，因为它催化两个醛的可逆不对称醛醇加成反应。为了扩大DERA的底物范围和立体选择性，已经研究了基于结构的底物设计以及位点特异性突变。以DERA的1.05 A晶体结构及其天然底物为指导，设计了5个定点突变体，以提高其与非天然非磷酸化底物D-2-脱氧核糖的活性。其中，在2-脱氧核糖的逆醛醇缩合反应中，S238D变体比野生型酶表现出2.5倍的改善。有趣的是 该S238D突变酶显示在连续的不对称醛醇缩合反应中以3-叠氮基丙醛为底物形成脱氧叠氮基乙基吡喃糖，它是相应内酯和降胆固醇剂立普妥的前体。该叠氮醛不是野生型酶的底物。新的非磷酸化底物的另一种基于结构的设计集中在使用野生型或S238D变体作为催化剂，2-甲基取代醛作为底物的对映体选择
• Inagaki, Journal of Biochemistry, 1940, vol. 32, p. 63,74,75
  作者：Inagaki

  DOI：——

  日期：——
• Deoxyribose-5-phosphate aldolase as a synthetic catalyst
  作者：Carlos F. Barbas、Yi Fong Wang、Chi Huey Wong

  DOI：10.1021/ja00161a064

  日期：1990.2
• Improvement of aldehyde tolerance and sequential aldol condensation activity of deoxyriboaldolase via immobilization on interparticle pore type mesoporous silica
  作者：Takayuki Y. Nara、Hideaki Togashi、Seigo Ono、Miki Egami、Chisato Sekikawa、Yo-hei Suzuki、Isao Masuda、Jun Ogawa、Nobuyuki Horinouchi、Sakayu Shimizu、Fujio Mizukami、Tatsuo Tsunoda

  DOI：10.1016/j.molcatb.2010.10.008

  日期：2011.2

  Deoxyriboaldolase from Klebsiella pneumonia (KpDERA) was immobilized on interparticle pore type mesoporous silica (IMS), which consists of aggregates of hexagonally close-packed silica nanoparticles. Incubation of the free KpDERA in 300 mM acetaldehyde resulted in a decrease in the free enzyme activity to 20% of the initial activity after incubation for 30 min. No activity was observed after 90 min incubation. In contrast, the IMS-immobilized KpDERA retained more than 50% of its activity after 30 min and 11% activity after 90 min incubation. The product yield of a sequential aldol condensation reaction, which is central to the production of pharmaceutically important intermediates, was found to be higher for IMS-immobilized KpDERA than for the free enzyme. These results suggest the potential utility of IMS as an immobilization support for DERA. (c) 2010 Elsevier B.V. All rights reserved.
• Pricer; Horecker, Biochemical Preparations, 1962, vol. 9, p. 35
  作者：Pricer、Horecker

  DOI：——

  日期：——