n-propyl α-L-arabinofuranoside | 121949-47-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: n-propyl α-L-arabinofuranoside
• 英文别名: propyl α-L-arabinofuranoside；propyl alpha-L-arabinofuranoside；(2S,3R,4R,5R)-2-(hydroxymethyl)-5-propoxyoxolane-3,4-diol
• CAS: 121949-47-1
• 化学式: C₈H₁₆O₅
• 分子量: 192.212
• InChiKey: YDCOTKHNXUISDD-RULNZFCNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.7
• 重原子数：
  13
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  79.2
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  β-cyclodextrin 、 n-propyl α-L-arabinofuranoside 在 Thermoanaerobacterium sp. cyclodextrin glucosyltransferase 作用下， 以 aq. phosphate buffer 为溶剂， 反应 72.0h， 以21%的产率得到propyl α-D-glucopyranosyl-(1,3)-α-L-arabinofuranoside
  参考文献：
  名称：

  Environmentally benign glycosylation of aryl pyranosides and aryl/alkyl furanosides demonstrating the versatility of thermostable CGTase from Thermoanaerobacterium sp.

  摘要：

  报道了Thermoanaerobacterium sp. CGTase对芳基呋喃苷的转糖基特异性。

  DOI：

  10.1039/c4gc00631c
• 作为产物：
  描述：

  L-阿拉伯糖 在 吡啶 、 sodium hydroxide 、 α-L-arabinofuranosidase (EC 3.2.1.55) 、 硫酸 、 ethanol; compound with boron fluoride 、 乙酰氯 作用下， 以 甲醇 、 二氯甲烷 、 水 、 溶剂黄146 为溶剂， 生成 n-propyl α-L-arabinofuranoside
  参考文献：
  名称：

  Enzymatic synthesis of alkyl arabinofuranosides using a thermostable α-l-arabinofuranosidase

  摘要：

  A thermostable alpha-L-arabinofuranosidase was tested for its ability to perform transglycosylation with different alcohol acceptors. Reactions were characterized by high rates with optimal synthesis being obtained within 10 min. Both primary and secondary alcohols could act as acceptors in transarabinosylation but yields of alkyl arabinosides decreased with increasing alkyl chain length. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0040-4039(02)02381-x

文献信息

• N.m.r. spectral study of α- and β-l-arabinofuranosides
  作者：Kenji Mizutani、Ryoji Kasai、Midori Nakamura、Osamu Tanaka、Hiromichi Matsuura

  DOI：10.1016/0008-6215(89)84018-2

  日期：1989.1

  -arabinofuranosides of various aliphatic alcohols were synthesized and then investigated by n.m.r. spectroscopy. The 13 C-n.m.r. glycosylation shift of these l -arabinofuranosides is very similar to that of l -arabinopyranosides and other glycopyranosides reported previously. The 3 J H-1,H-2 value of these α- l -arabinofuranosides is significantly different from that of the β anomers and can be used

  摘要合成了各种脂肪醇的1-阿拉伯呋喃糖苷的端基异构对，然后通过核磁共振波谱研究。这些1-阿拉伯呋喃糖苷的13 Cn.mr糖基化转变与先前报道的1-阿拉伯吡喃果糖苷和其他糖吡喃糖苷的转变非常相似。这些α-1-阿拉伯呋喃糖苷的3 J H-1，H-2值与β端基异构体的3 J H-1，H-2值显着不同，可用于确定端基构型。然而，与糖吡喃糖苷的情况相反，1-阿拉伯呋喃糖苷的每个异头异构系列的1 J C-1，H-1值彼此非常相似。还通过核磁共振波谱研究了一些含有1-阿拉伯呋喃糖苷单元的二糖。
• Araf51 with improved transglycosylation activities: one engineered biocatalyst for one specific acceptor
  作者：Alizé Pennec、Richard Daniellou、Pascal Loyer、Caroline Nugier-Chauvin、Vincent Ferrières

  DOI：10.1016/j.carres.2014.10.031

  日期：2015.1

  were selected on their ability to catalyze the transglycosylation reaction of p-nitrophenyl α-L-arabinofuranoside (pNP-Araf) used as a donor and various aliphatic alcohols as acceptors. This screening strategy underlined 5 interesting clones, each one corresponding to one acceptor. They appeared to be much more efficient in the transglycosylation reaction compared to the wild type enzyme whereas no self-condensation

  为了获得用于合成烷基阿拉伯呋喃糖苷的有效生物催化剂，已经进行了阿拉伯呋喃呋喃糖基水解酶Araf51的随机诱变。选择突变体是基于其催化用作供体的对硝基苯基α-L-阿拉伯呋喃糖苷（pNP-Araf）和各种脂族醇作为受体的转糖基化反应的能力。这种筛选策略强调了5个有趣的克隆，每个克隆对应一个受体。与野生型酶相比，它们在转糖基化反应中似乎更有效，而未检测到自缩合或水解产物。此外，突变体对已为其选择了醇的高特异性证实了筛选过程。突变酶的序列分析表明，
• MIZUTANI, KENJI;KASAI, RYOJI;NAKAMURA, MIDORI;TANAKA, OSAMU;MATSUURA, HIR+, CARBOHYDR. RES., 185,(1989) N, C. 27-38
  作者：MIZUTANI, KENJI、KASAI, RYOJI、NAKAMURA, MIDORI、TANAKA, OSAMU、MATSUURA, HIR+

  DOI：——

  日期：——
• ONE STEP ENZYMATIC PROCESS FOR PRODUCING ALKYL FURANOSIDES
  申请人：Ecole Nationale Supérieure de Chimie de Rennes

  公开号：EP2841587A1

  公开（公告）日：2015-03-04
• [EN] ONE STEP ENZYMATIC PROCESS FOR PRODUCING ALKYL FURANOSIDES<br/>[FR] PROCÉDÉ ENZYMATIQUE À UNE ÉTAPE POUR LA FABRICATION D'ALKYL FURANOSIDES
  申请人：ENSCR

  公开号：WO2013160205A1

  公开（公告）日：2013-10-31

  The present invention relates to a process for enzymatically converting a furanoside substrate in a product of interest, comprising contacting said substrate with an enzyme in presence of an alcohol acceptor, wherein said enzyme is preferably Araf51, and wherein said product is preferably an alkyl furanoside. The present invention also relates to mutant Araf51 enzyme showing improved transglycosylation activity in comparison with the native wild-type (wt) Araf51 enzyme, and to a method for screening said mutants.