(3S,4R)-5-[N-(benzyloxycarbonyl)amino]-1,5-dideoxypent-2-ulose | 1159196-57-2

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: (3S,4R)-5-[N-(benzyloxycarbonyl)amino]-1,5-dideoxypent-2-ulose
• 英文别名: benzyl N-[(2R,3S)-2,3-dihydroxy-4-oxopentyl]carbamate
• CAS: 1159196-57-2
• 化学式: C₁₃H₁₇NO₅
• 分子量: 267.282
• InChiKey: VIHGNLIDNMKJJF-VXGBXAGGSA-N

物化性质

• 沸点：
  512.5±50.0 °C(Predicted)
• 密度：
  1.272±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.1
• 重原子数：
  19
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  95.9
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  (3S,4R)-5-[N-(benzyloxycarbonyl)amino]-1,5-dideoxypent-2-ulose 在 10% Pd/C 、 氢气 作用下， 生成 1,4,5-trideoxy-1,4-imino-D-arabinitol
  参考文献：
  名称：

  In situ aldehyde generation for aldol addition reactions catalyzed by d-fructose-6-phosphate aldolase

  摘要：

  In situ coupling of aldehyde generation, by a mild alcohol oxidation, with an enzymatic aldol addition reaction, mediated by D-fructose-6-phosphate aldolase (FSA) has been investigated as an approach to improve the performance of the process. Four sustainable oxidation methods compatible with the activity and stability of the enzymatic aldol addition have been assayed. Among them, the laccase/O-2/2,2,6,6-tetramethylpiperidine-N-oxyl (TEMPO) and alcohol oxidase gave the best results for the N-Cbz-aminoethanol to N-Cbz-glycinal (53%) and furfuryl alcohol to furfural (89%), respectively, followed by the aldol addition with hydroxyacetone catalyzed by FSA A129S mutant. (C) 2012 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.molcatb.2012.02.001
• 作为产物：
  描述：

  2-苄氧羰基氨基-1-乙醇 在 2,2,6,6-四甲基哌啶氧化物 、 Trametes versicolor laccase 、 Escherichia coli D-fructose-6-phosphate aldolase A₁₂₉S/A₁₆₅G mutant 、 氧气 作用下， 以 乙酸乙酯 、 甲苯 为溶剂， 25.0 ℃ 、202.66 kPa 条件下， 反应 27.0h， 生成 (3S,4R)-5-[N-(benzyloxycarbonyl)amino]-1,5-dideoxypent-2-ulose
  参考文献：
  名称：

  In situ aldehyde generation for aldol addition reactions catalyzed by d-fructose-6-phosphate aldolase

  摘要：

  In situ coupling of aldehyde generation, by a mild alcohol oxidation, with an enzymatic aldol addition reaction, mediated by D-fructose-6-phosphate aldolase (FSA) has been investigated as an approach to improve the performance of the process. Four sustainable oxidation methods compatible with the activity and stability of the enzymatic aldol addition have been assayed. Among them, the laccase/O-2/2,2,6,6-tetramethylpiperidine-N-oxyl (TEMPO) and alcohol oxidase gave the best results for the N-Cbz-aminoethanol to N-Cbz-glycinal (53%) and furfuryl alcohol to furfural (89%), respectively, followed by the aldol addition with hydroxyacetone catalyzed by FSA A129S mutant. (C) 2012 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.molcatb.2012.02.001

文献信息

• <scp>D</scp>-Fructose-6-phosphate Aldolase in Organic Synthesis: Cascade Chemical-Enzymatic Preparation of Sugar-Related Polyhydroxylated Compounds
  作者：Alda Lisa Concia、Carles Lozano、José A. Castillo、Teodor Parella、Jesús Joglar、Pere Clapés

  DOI：10.1002/chem.200802532

  日期：2009.4.6

  D‐Fructose‐6‐phosphate aldolase (FSA) is a key biocatalyst for the alternative synthetic construction of biologically active products with known therapeutic and research interest or novel structures relevant to drug discovery. Novel aldol addition reactions of dihydroxyacetone and hydroxyacetone to a variety of aldehydes catalyzed by FSA are presented (see scheme).

  D-果糖-6-磷酸醛缩酶（FSA）是具有已知治疗和研究兴趣或与药物开发相关的新颖结构的生物活性产品的替代合成构造的关键生物催化剂。提出了新颖的二羟基丙酮和羟丙酮与FSA催化的各种醛的醛醇加成反应（参见方案）。
• Structure-guided redesign of d-fructose-6-phosphate aldolase from E. coli: remarkable activity and selectivity towards acceptor substrates by two-point mutation
  作者：Mariana Gutierrez、Teodor Parella、Jesús Joglar、Jordi Bujons、Pere Clapés

  DOI：10.1039/c1cc11069a

  日期：——

  Structure-guided re-design of the acceptor binding site of D-fructose-6-phosphate aldolase from E. coli leads to the construction of FSA A129S/A165G double mutant with an activity between 5- to >900-fold higher than that of wild-type towards N-Cbz-aminoaldehyde derivatives.

  通过重新设计大肠杆菌 D-果糖-6-磷酸醛缩酶的受体结合位点，构建了 FSA A129S/A165G 双突变体，其对 N-苄氧羰基氨基醛衍生物的活性比野生型高出 5 到 900 倍。