(3S,4R)-6-[(benzyloxycarbonyl)amino]-5,6-dideoxyhex-2-ulose | 121742-14-1

• 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)-6-[(benzyloxycarbonyl)amino]-5,6-dideoxyhex-2-ulose
• 英文别名: benzyl N-[(3R,4S)-3,4,6-trihydroxy-5-oxohexyl]carbamate
• CAS: 121742-14-1
• 化学式: C₁₄H₁₉NO₆
• 分子量: 297.308
• InChiKey: NNFRVRHUZOYOAH-YPMHNXCESA-N

物化性质

• 沸点：
  589.8±50.0 °C(Predicted)
• 密度：
  1.327±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.4
• 重原子数：
  21
• 可旋转键数：
  9
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  116
• 氢给体数：
  4
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  (3S,4R)-6-[(benzyloxycarbonyl)amino]-5,6-dideoxyhex-2-ulose 在 palladium on activated charcoal 氢气 作用下， 以 甲醇 、 水 为溶剂， 反应 24.0h， 生成 Fagomine; 桑叶生物碱; (2R,3R,4R)-2-羟甲基哌啶-3,4-二醇
  参考文献：
  名称：

  Pederson, Richard L.; Wong, Chi-Huey, Heterocycles, 1989, vol. 28, # 1, p. 477 - 480

  摘要：

  DOI：
• 作为产物：
  描述：

  3-(苄氧羰基氨基)-1-丙醇 在 pyridinium chlorochromate 作用下， 反应 36.0h， 生成 (3S,4R)-6-[(benzyloxycarbonyl)amino]-5,6-dideoxyhex-2-ulose
  参考文献：
  名称：

  Pederson, Richard L.; Wong, Chi-Huey, Heterocycles, 1989, vol. 28, # 1, p. 477 - 480

  摘要：

  DOI：

文献信息

• A new concept for production of (3S,4R)-6-[(benzyloxycarbonyl)amino]-5,6-dideoxyhex-2-ulose, a precursor of <scp>d</scp>-fagomine
  作者：Martina Sudar、Zvjezdana Findrik、Đurđa Vasić-Rački、Anna Soler、Pere Clapés

  DOI：10.1039/c5ra14414k

  日期：——

  A novel cascade reaction combining three enzymes in one pot for the production of aldol adduct (3S,4R)-6-[(benzyloxycarbonyl)amino]-5,6-dideoxyhex-2-ulose was studied and 79% yield on aldol adduct was achieved in the batch reactor.

  一种新型级联反应，在一个反应器中结合三种酶，用于生产戊糖醛缩合物(3S,4R)-6-[(苄氧羰基)氨基]-5,6-二去氧己-2-烯醛，并在批量反应器中实现了对戊糖醛缩合物的79%产率。
• Synthesis of non-natural carbohydrates from glycerol and aldehydes in a one-pot four-enzyme cascade reaction
  作者：Lara Babich、Lieke J. C. van Hemert、Aleksandra Bury、Aloysius F. Hartog、Pierpaolo Falcicchio、John van der Oost、Teunie van Herk、Ron Wever、Floris P. J. T. Rutjes

  DOI：10.1039/c1gc15429j

  日期：——

  A simple procedure has been developed for the synthesis of enantio- and diastereomerically pure carbohydrate analogues from glycerol and a variety of aldehydes in one pot using a four-enzyme cascade reaction. As a proof of concept of the usefulness of this enzymatic catalytic cascade the naturally occurring azasugarD-fagomine was synthesized. This work highlights the potential value of using enzymes in cascade reactions to selectively form complex products that by previous traditional organic chemistry could only be obtained via repeated isolation and purification of intermediates.

  已经开发出一种简单的程序，用于通过四酶级联反应在一个反应瓶中从甘油和多种醛类合成对映体和非对映体纯的糖类类似物。作为这种酶催化级联反应有用性的概念验证，合成了天然存在的氨基糖D-fagomine。这项工作强调了在级联反应中使用酶的潜在价值，以选择性地形成复杂产物，而这些产物在以往传统有机化学中只能通过反复分离和纯化中间体获得。
• Fructose-6-phosphate Aldolase in Organic Synthesis:  Preparation of <scp>d</scp>-Fagomine, <i>N</i>-Alkylated Derivatives, and Preliminary Biological Assays
  作者：José A. Castillo、Jordi Calveras、Josefina Casas、Montserrat Mitjans、M. Pilar Vinardell、Teodor Parella、Tomoyuki Inoue、Georg A. Sprenger、Jesús Joglar、Pere Clapés

  DOI：10.1021/ol0625482

  日期：2006.12.1

  straightforward two-step chemo-enzymatic synthesis of D-fagomine and some of its N-alkylated derivatives in 51% isolated yield and 99% de. The key step is the FSA-catalyzed aldol addition of simple dihydroxyacetone (DHA) to N-Cbz-3-aminopropanal. The use of FSA greatly simplifies the enzymatic procedures that used dihydroxyacetonephosphate or DHA/esters. Some N-alkyl derivatives synthesized elicited antifungal

  [结构：见正文] D-果糖-6-磷酸醛缩酶（FSA）以51％的分离产率和99％的de介导了D-fagomine及其某些N-烷基化衍生物的新颖，简单的两步化学酶法合成。关键步骤是在N-Cbz-3-氨基丙醛中FSA催化的简单二羟丙酮（DHA）的羟醛加成。FSA的使用大大简化了使用磷酸二羟基丙酮磷酸酯或DHA /酯的酶促程序。合成的一些N-烷基衍生物引起了抗真菌和抗菌活性以及增强的抑制活性，以及​​对β-半乳糖苷酶和α-葡萄糖苷酶的选择性。
• 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。
• <scp>d</scp>-Fructose-6-Phosphate Aldolase-Catalyzed One-Pot Synthesis of Iminocyclitols
  作者：Masakazu Sugiyama、Zhangyong Hong、Pi-Hui Liang、Stephen M. Dean、Lisa J. Whalen、William A. Greenberg、Chi-Huey Wong

  DOI：10.1021/ja073911i

  日期：2007.11.28

  A one-pot chemoenzymatic method for the synthesis of a variety of new iminocyclitols from readily available, non-phosphorylated donor substrates has been developed. The method utilizes the recently discovered fructose-6-phosphate aldolase (FSA), which is functionally distinct from known aldolases in its tolerance of different donor substrates as well as acceptor substrates. Kinetic studies were performed with dihydroxyacetone (DHA), the presumed endogenous substrate for FSA, as well as hydroxy acetone (HA) and 1-hydroxy-2-butanone (HB) as donor substrates, in each case using glyceraidehyde-3-phosphate as acceptor substrate. Remarkably, FSA used the three donor substrates with equal efficiency, with k(cat)/K-M-values of 33, 75, and 20 M-1 s(-1), respectively. This level of donor substrate tolerance is unprecedented for an aldolase. Furthermore, DHA, HA, and HB were accepted as donors in FSA-catalyzed aldol reactions with a variety of azido- and Cbz-amino aldehyde acceptors. The broad substrate tolerance of FSA and the ability to circumvent the need for phosphorylated substrates allowed for one-pot synthesis of a number of known and novel iminocyclitols in good yields, and in a very concise fashion. New iminocyclitols were assayed as inhibitors against a panel of glycosidases. Compounds 15 and 16 were specific alpha-mannosidase inhibitors, and 24 and 26 were potent and selective inhibitors of beta-N-acetylglucosaminidases in the submicromolar range. Facile access to these compounds makes them attractive core structures for further inhibitor optimization.