D-galactopyranose 1-phosphate

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: D-galactopyranose 1-phosphate
• 英文别名: D-galactose 1-phosphate；D-galactose-1-phosphate；galactose 1-phosphate；galactose-1-phosphate；glucose-1-phosphate；Gal-1-P；[(3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl] dihydrogen phosphate
• 化学式: C₆H₁₃O₉P
• 分子量: 260.138
• InChiKey: HXXFSFRBOHSIMQ-SVZMEOIVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.8
• 重原子数：
  16
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  157
• 氢给体数：
  6
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  D-galactopyranose 1-phosphate 在 D-galactosyl-β1–3-N-acetyl-D-hexosamine phosphorylase 、 Neisseria meningitides CMP-Sia synthetase 、 Pasteurella multocida α2,3-sialyltransferase 、 magnesium 、 胞苷-5’-三磷酸 作用下， 以 aq. buffer 为溶剂， 生成 Neu5Acα(2-3)Galβ(1-3)GalNAc
  参考文献：
  名称：

  Two-Step Chemoenzymatic Detection of N-Acetylneuraminic Acid−α(2-3)-Galactose Glycans

  摘要：

  Sialic acids are typically linked alpha(2-3) or alpha(2-6) to the galactose that located at the non-reducing terminal end of glycans, playing important but distinct roles in a variety of biological and pathological processes. However, details about their respective roles are still largely unknown due to the lack of an effective analytical technique. Herein, a two-step chemoenzymatic approach for the rapid and sensitive detection of N-acetylneuraminic acid-alpha(2-3)-galactose glycans is described.

  DOI：

  10.1021/jacs.6b07132
• 作为产物：
  描述：

  口服葡萄糖 在 galactose kinase from Bifidobacterium infantis 作用下， 生成 D-galactopyranose 1-phosphate
  参考文献：
  名称：

  Two-Step Chemoenzymatic Detection of N-Acetylneuraminic Acid−α(2-3)-Galactose Glycans

  摘要：

  Sialic acids are typically linked alpha(2-3) or alpha(2-6) to the galactose that located at the non-reducing terminal end of glycans, playing important but distinct roles in a variety of biological and pathological processes. However, details about their respective roles are still largely unknown due to the lack of an effective analytical technique. Herein, a two-step chemoenzymatic approach for the rapid and sensitive detection of N-acetylneuraminic acid-alpha(2-3)-galactose glycans is described.

  DOI：

  10.1021/jacs.6b07132

文献信息

• Isolation and Properties of Glucose-1-phosphatase from Mycelia of<i>Pholiota nameko</i>
  作者：Toshio JOH、Junshi YAZAKI、Kayo SUZUKI、Toshiro HAYAKAWA

  DOI：10.1271/bbb.62.2251

  日期：1998.1

  An acid phosphatase with a very high substrate specificity for glucose-1-phosphate was isolated for the first time from mycelia of Pholiota nameko. The molecular weight of the enzyme was estimated to be 31,000 on gel filtration and 35,000 on SDS-PAGE. The activity was inhibited by Cu2+, Hg2+, molybdate, and tartaric acid. The sequence of N-terminal 20 amino acid residues was analyzed.

  首次从 Pholiota nameko 的菌丝体中分离出一种对 1-磷酸葡萄糖具有极高底物特异性的酸性磷酸酶。经凝胶过滤测定，该酶的分子量为 31 000，经 SDS-PAGE 测定，分子量为 35 000。该酶的活性受 Cu2+、Hg2+、钼酸盐和酒石酸的抑制。对 N 端 20 个氨基酸残基的序列进行了分析。
• Substrate specificity of galactokinase from Streptococcus pneumoniae TIGR4 towards galactose, glucose, and their derivatives
  作者：Yang Zou、Wenjun Wang、Li Cai、Leilei Chen、Mengyang Xue、Xiaomei Zhang、Jie Shen、Min Chen

  DOI：10.1016/j.bmcl.2012.03.095

  日期：2012.5

  Galactokinases (GalKs) have attracted significant research attention for their potential applications in the enzymatic synthesis of unique sugar phosphates. The galactokinase (GalKSpe4) cloned from Streptococcus pneumoniae TIGR4 presents a remarkably broad substrate range including 14 diverse natural and unnatural sugars. TLC and MS studies revealed that GalKSpe4 had relaxed activity towards galactose derivatives with modifications on the C-6, 4- or 2-positions. Additionally, GalKSpe4 can also tolerate glucose while glucose derivatives with modifications on the C-6, 4- or 2-positions were unacceptable. More interestingly, GalKSpe4 can phosphorylate L-mannose in moderate yield (43%), while other L-sugars such as L-Gal cannot be recognized by this enzyme. These results are very significant because there is rarely enzyme reported that can phosphorylate such uncommon substrates as L-mannose. (C) 2012 Elsevier Ltd. All rights reserved.
• Wong, Chi-Huey; Schuster, Matthias; Wang, Peng, Journal of the American Chemical Society, 1993, vol. 115, # 14, p. 5893 - 5898
  作者：Wong, Chi-Huey、Schuster, Matthias、Wang, Peng、Sears, Pamela

  DOI：——

  日期：——
• Leishmania UDP-sugar Pyrophosphorylase
  作者：Sebastian Damerow、Anne-Christin Lamerz、Thomas Haselhorst、Jana Führing、Patricia Zarnovican、Mark von Itzstein、Françoise H. Routier

  DOI：10.1074/jbc.m109.067223

  日期：2010.1

  The Leishmania parasite glycocalyx is rich in galactose-containing glycoconjugates that are synthesized by specific glycosyltransferases that use UDP-galactose as a glycosyl donor. UDP-galactose biosynthesis is thought to be predominantly a de novo process involving epimerization of the abundant nucleotide sugar UDP-glucose by the UDP-glucose 4-epimerase, although galactose salvage from the environment has been demonstrated for Leishmania major. Here, we present the characterization of an L. major UDP-sugar pyrophosphorylase able to reversibly activate galactose 1-phosphate into UDP-galactose thus proving the existence of the Isselbacher salvage pathway in this parasite. The ordered bisubstrate mechanism and high affinity of the enzyme for UTP seem to favor the synthesis of nucleotide sugar rather than their pyrophosphorolysis. Although L. major UDP-sugar pyrophosphorylase preferentially activates galactose 1-phosphate and glucose 1-phosphate, the enzyme is able to act on a variety of hexose 1-phosphates as well as pentose 1-phosphates but not hexosamine 1-phosphates and hence presents a broad in vitro specificity. The newly identified enzyme exhibits a low but significant homology with UDP-glucose pyrophosphorylases and conserved in particular is the pyrophosphorylase consensus sequence and residues involved in nucleotide and phosphate binding. Saturation transfer difference NMR spectroscopy experiments confirm the importance of these moieties for substrate binding. The described leishmanial enzyme is closely related to plant UDP-sugar pyrophosphorylases and presents a similar substrate specificity suggesting their common origin.
• US4792615A
  申请人：——

  公开号：US4792615A

  公开（公告）日：1988-12-20