[5-(2-氨基-6-氧代-3,6-二氢-9H-嘌呤-9-基)-3,4-二羟基四氢-2-呋喃基]甲基 3,4,5-三羟基-6-(羟基甲基)四氢-2H-吡喃-2-基二氢二磷酸酯 | 6815-91-4

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷酸
• 中文名称: [5-(2-氨基-6-氧代-3,6-二氢-9H-嘌呤-9-基)-3,4-二羟基四氢-2-呋喃基]甲基 3,4,5-三羟基-6-(羟基甲基)四氢-2H-吡喃-2-基二氢二磷酸酯
• 中文别名: [5-(2-氨基-6-氧代-3,6-二氢-9H-嘌呤-9-基)-3,4-二羟基四氢-2-呋喃基]甲基3,4,5-三羟基-6-(羟基甲基)四氢-2H-吡喃-2-基二氢二磷酸酯；GDP-L-半乳糖钠盐
• 英文名称: GDP-L-galactose
• 英文别名: GDP-beta-L-galactose；[[(2R,3S,4R,5R)-5-(2-amino-6-oxo-1H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(2R,3S,4R,5S,6S)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl] hydrogen phosphate
• CAS: 6815-91-4
• 化学式: C₁₆H₂₅N₅O₁₆P₂
• 分子量: 605.346
• InChiKey: MVMSCBBUIHUTGJ-JGQUBWHWSA-N

物化性质

• 密度：
  2.51±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -6.2
• 重原子数：
  39
• 可旋转键数：
  9
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.69
• 拓扑面积：
  327
• 氢给体数：
  10
• 氢受体数：
  18

反应信息

• 作为反应物：
  描述：

  β-D-Galp-(1->3)-β-D-Galp-O-CH3 、 [5-(2-氨基-6-氧代-3,6-二氢-9H-嘌呤-9-基)-3,4-二羟基四氢-2-呋喃基]甲基 3,4,5-三羟基-6-(羟基甲基)四氢-2H-吡喃-2-基二氢二磷酸酯 在 Helix pomatia albumen gland sediment sodium azide 、 calf intestine alkaline phosphatase EC 3.1.3.1 、 manganese(ll) chloride 作用下， 以 various solvent(s) 为溶剂， 反应 18.0h， 生成 L-Gal(a1-2)Gal(b1-3)b-Gal1Me
  参考文献：
  名称：

  Enzymatic α(1→2)-l-fucosylation: investigation of the specificity of the α(1→2)-l-galactosyltransferase from Helix pomatia

  摘要：

  The alpha(1-->2)-L-galactosyltransferase from Helix pomatia transfers an L-fucosyl residue from GDP-L-Fucose to a terminal, non-reducin D-galactopyranosyl moiety of an oligosaccharide. The extent of the enzyme's specificity towards the stereochemistry at the D-galactopyranosyl anomeric centre, the site of interglycosidic linkage and the nature of the subterminal oliaosaccharide residue has been investigated using HPAEC-PAD and MALDI-TOF technology. This alpha(1-->2)-L-galactosyltransferase is specific for D-galactopyranosyl beta-linkages, independent of the site of the interglycosidic linkage and aglycone configuration and with limited specificity for the nature of the subterminal sugar residue. (C) 2003 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/s0957-4166(03)00521-4
• 作为产物：
  描述：

  guanosine 5'-diphospho-D-mannose 在 Tris-HCl buffer 、 nicotinamide adenine dinucleotide 作用下， 生成 GDP-L-gulose 、 [5-(2-氨基-6-氧代-3,6-二氢-9H-嘌呤-9-基)-3,4-二羟基四氢-2-呋喃基]甲基 3,4,5-三羟基-6-(羟基甲基)四氢-2H-吡喃-2-基二氢二磷酸酯
  参考文献：
  名称：

  Characterization of a GDP-d-mannose 3″,5″-epimerase from rice

  摘要：

  The enzymatic characterization of GDP-D-mannose 3",5"-epimerase (GME), a key enzyme in the biosynthesis of vitamin C in plants is described. The GME gene (Genbank Accession No. AB 193582) in rice was cloned, and expressed as a fusion protein in Escherichia coli. Reaction products from GDP-D-mannose, as produced by GME catalysis, were separated by recycling HPLC on an ODS column, and were determined to be GDP-L-galactose and GDP-L-gulose, based on their NMR spectra and sugar analysis. The reaction catalyzed by GME was inhibited by GDP, and was strongly accelerated by NAD(+) in contrast to the case of GME from Arabidopsis thaliana. This difference in the effect of NAD(+) on GME activity can be attributed to the NAD binding domain which is conserved in the rice gene, but not in the Arabidopsis thaliana gene. The apparent K-m and k(cat) were determined to be 1.20 x 10(-5) M and 0.127 s(-1), respectively, in the presence of 20 mu M NAD(+). The fractions of GDP-D-mannose, GDP-L-galactose and GDP-L-gulose, at equilibrium, were approximately 0.75, 0.20 and 0.05, respectively. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.phytochem.2005.12.003

文献信息

• Chemoenzymatic synthesis of l-galactosylated dimeric Sialyl Lewis X structures employing α-1,3-fucosyltransferase V
  作者：Arno Düffels、Luke G. Green、Roman Lenz、Steven V. Ley、Stephane P. Vincent、Chi-Huey Wong

  DOI：10.1016/s0968-0896(00)00187-5

  日期：2000.10

  L-Galactosylated dimeric sialyl Lewis X (SLeX) has been prepared employing a combination of chemical and enzymatic synthetic methods. GDP-L-galactose has been chemically synthesised. Enzymatic transfer of L-galactose onto the acceptor (Sia-alpha2,3-Gal-beta1,4-GlcNAc-beta1,3/6)2-Man-alpha1-OMe was achieved using the human alpha-1,3-fucosyltransferase V.

  L-半乳糖基化的二聚唾液酸路易斯X（SLeX）已采用化学和酶促合成方法的组合制备。GDP-L-半乳糖已化学合成。使用人alpha-1,3-岩藻糖基转移酶V将L-半乳糖酶转移到受体（Sia-alpha2,3-Gal-beta1,4-GlcNAc-beta1,3 / 6）2-Man-alpha1-OMe上。
• Effective Synthesis of Guanosine 5′-Diphospho-β-<scp>l</scp>-galactose Using Bacterial<scp>l</scp>-Fucokinase/Guanosine 5′-Diphosphate-<scp>l</scp>-fucose Pyrophosphorylase
  作者：Hiroyuki Ohashi、Claudia Wahl、Takao Ohashi、Lothar Elling、Kazuhito Fujiyama

  DOI：10.1002/adsc.201700901

  日期：2017.12.11

  5′‐triphosphate (ATP) and guanosine 5′‐triphosphate (GTP). A high synthesis yield was obtained after screening of the optimum FKP reaction conditions in a 96‐well format and analysis by multiplexed capillary electrophoresis (MP‐CE). Conversion of l‐Gal substrate yielded 97% GDP‐l‐Gal using purified recombinant FKP expressed in E. coli. Moreover, GDP‐l‐Gal was successfully purified with 92% (34.5 mg) overall yield

  核苷酸糖鸟苷5'-二磷酸-β-升半乳糖（GDP-升-Gal）被称为所述的关键中间体升植物和藻类的抗坏血酸生物合成途径。此外，GDP-升-Gal充当的施主衬底升-galactosyltransferase，其转让升-Gal上的糖缀合物的非还原末端。为了合成品种升含-Gal-糖缀合物和探索新的升-galactosyltransferases，GDP-升待制备-Gal需求，因为它不是可商购的。在植物中，GDP- d-甘露糖-3'，5'-表异构酶（GME）转换GDP-α- d-甘露糖（GDP- d- Man ）到GDP- l- Gal和GDP- l- gulose。GDPl - Gal以前是使用GME和GDP- d- Man来准备的，因此均衡比率相对于GDP- d- Man有偏差。在这项研究中，有效的GDP-升从-Gal生产升-Gal使用细菌建立升-fucokinase / GDP-升岩藻糖焦磷酸
• Depre, Dominique; Dueffels, Arno; Green, Luke G., Chemistry - A European Journal, 1999, vol. 5, # 11, p. 3326 - 3340
  作者：Depre, Dominique、Dueffels, Arno、Green, Luke G.、Lenz, Roman、Ley, Steven V.、Wong, Chi-Huey

  DOI：——

  日期：——
• Fucosyltransferase-catalyzed formation of l-galactosylated Lewis structures
  作者：Katja Stangier、Monica M. Palcic、David R. Bundle、Ole Hindsgaul、Joachim Thiem

  DOI：10.1016/s0008-6215(97)10031-3

  日期：1997.12

  The Lewis (alpha 1-3/4) fucosyltransferase isolated from human milk could be used for preparative fucosylations of the disaccharide accepters Gal(beta 1-3)GlcNAc(beta 1-0)R (at position OH-4) and Gal(beta 1-4)GlcNAc(beta 1-0)R (at position OH-3) [R = (CH2)(8)COOMe]. As donors GDP-L-Gal and deoxygenated derivatives were used to lead to a series of novel modified trisaccharides of the Lewis(a) and the Lewis(x) type, respectively. (C) 1998 Elsevier Science Ltd.
• Characterization of a GDP-d-mannose 3″,5″-epimerase from rice
  作者：Kentaroh Watanabe、Kiyoshi Suzuki、Shinichi Kitamura

  DOI：10.1016/j.phytochem.2005.12.003

  日期：2006.2

  The enzymatic characterization of GDP-D-mannose 3",5"-epimerase (GME), a key enzyme in the biosynthesis of vitamin C in plants is described. The GME gene (Genbank Accession No. AB 193582) in rice was cloned, and expressed as a fusion protein in Escherichia coli. Reaction products from GDP-D-mannose, as produced by GME catalysis, were separated by recycling HPLC on an ODS column, and were determined to be GDP-L-galactose and GDP-L-gulose, based on their NMR spectra and sugar analysis. The reaction catalyzed by GME was inhibited by GDP, and was strongly accelerated by NAD(+) in contrast to the case of GME from Arabidopsis thaliana. This difference in the effect of NAD(+) on GME activity can be attributed to the NAD binding domain which is conserved in the rice gene, but not in the Arabidopsis thaliana gene. The apparent K-m and k(cat) were determined to be 1.20 x 10(-5) M and 0.127 s(-1), respectively, in the presence of 20 mu M NAD(+). The fractions of GDP-D-mannose, GDP-L-galactose and GDP-L-gulose, at equilibrium, were approximately 0.75, 0.20 and 0.05, respectively. (c) 2005 Elsevier Ltd. All rights reserved.