glucose-6-phosphate | 76939-52-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: glucose-6-phosphate
• 英文别名: aldehydo-D-glucose 6-phosphate(2-)；[(2R,3R,4S,5R)-2,3,4,5-tetrahydroxy-6-oxohexyl] phosphate
• CAS: 76939-52-1
• 化学式: C₆H₁₁O₉P
• 分子量: 258.122
• InChiKey: VFRROHXSMXFLSN-SLPGGIOYSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  -4.7
• 重原子数：
  16
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  170
• 氢给体数：
  4
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  glucose-6-phosphate 生成 D-glucitol 6-phosphate
  参考文献：
  名称：

  Identification and quantification of methyl ester groups in methylated sugar acids and phosphates by g.l.c.-m.s. after alkaline transesterification with sodium ethoxide

  摘要：

  DOI：

  10.1016/s0008-6215(00)90065-x
• 作为产物：
  描述：

  葡萄糖 在 hexokinase from Shewanella woodyi 、 adenosine 5'-triphosphate 、 magnesium chloride 作用下， 以 aq. phosphate buffer 为溶剂， 反应 24.0h， 生成 glucose-6-phosphate
  参考文献：
  名称：

  The Shewanella woodyi galactokinase pool phosphorylates glucose at the 6-position

  摘要：

  Galactokinases are a class of enzymes which belong to the GHMP (galactokinase, homoserine kinase, mevalonate kinase, and phosphomevalonate kinase) superfamily and catalyse the phosphorylation of galactose in the first step of the Leloir pathway. Here we report the discovery of three enzymes from Shewanella woodyi which have been classified as galactokinases based on sequence similarity. However, each of these enzymes show little to no significant activity towards galactose and instead exhibit a strong preference for glucose. Furthermore, in contrast to the usual galactose-1-phosphate product of the galactokinase-catalysed reaction, these enzymes produce glucose-6-phosphate. This radical change in enzyme functionality is postulated to be linked to the mutation of a glycine residue which is conserved in all other sequenced galactokinases. (C) 2017 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2017.10.018

文献信息

• Characterization and Partial Purification of Aldose-6-phosphate Reductase (Alditol-6-Phosphate:NADP 1-Oxidoreductase) from Apple Leaves
  作者：Fayek B. Negm、Wayne H. Loescher

  DOI：10.1104/pp.67.1.139

  日期：1981.1.1

  (alditol 6-phosphate:NADP 1-oxidoreductase) was isolated and characterized from mature apple leaves (Malus domestica cv. Starkrimson). The enzyme was purified 79-fold. The enzyme catalyzed the following reversible reaction: d-glucose 6-phosphate + NADPH + H(+) right arrow over left arrow d-sorbitol 6-phosphate + NADP(+). No activity was detected when NAD(+) was substituted for NADP(+) or when NADH was

  6-磷酸醛糖还原酶（6-磷酸醛糖醇：NADP 1-氧化还原酶）是从成熟的苹果叶（Malusdomestica cv.Starkrimson）中分离出来并表征的。该酶被纯化了 79 倍。该酶催化以下可逆反应：d-葡萄糖 6-磷酸 + NADPH + H(+) 右箭头超过左箭头 d-山梨糖醇 6-磷酸 + NADP(+)。当 NAD(+) 替代 NADP(+) 或 NADH 替代 NADPH 时，未检测到活性。该酶以比 d-葡萄糖 6-磷酸更高的速率减少 d-半乳糖 6-磷酸。d-甘露糖 6-磷酸和 2-脱氧-d-葡萄糖 6-磷酸以低速率减少。d-葡萄糖 1-磷酸、d-果糖 6-磷酸、d-核糖 5-磷酸、d-葡萄糖和山梨糖醇不用作底物。d-山梨糖醇 6-磷酸氧化和 d-葡萄糖 6-磷酸还原的最适 ​​pH 值为 9.5。d-山梨糖醇 6-磷酸氧化和 d-葡萄糖 6-磷酸还原的 K(m) 值分别为
• Magnesium-dependent Phosphatase-1 Is a Protein-Fructosamine-6-phosphatase Potentially Involved in Glycation Repair
  作者：Juliette Fortpied、Pushpa Maliekal、Didier Vertommen、Emile Van Schaftingen

  DOI：10.1074/jbc.m513208200

  日期：2006.7

  Fructosamine-3-kinase (FN3K) is a recently described protein-repair enzyme responsible for the removal of fructosamines, which are the products of a spontaneous reaction of glucose with amines. We show here that, compared with glucose, glucose 6-phosphate (Glu-6-P) reacted 3-6-fold more rapidly with proteins and 8-fold more rapidly with N-alpha-t-Boc-lysine, being therefore a more significant intracellular glycating agent than glucose in skeletal muscle and heart. Fructosamine 6-phosphates, which result from the reaction of amines with Glu-6-P, were not substrates for FN3K. However, a phosphatase that dephosphorylates protein-bound fructosamine 6-phosphates was found to be present in rat tissues. This enzyme was purified to near homogeneity from skeletal muscle and was identified as magnesium-dependent phosphatase-1 (MDP-1), an enzyme of the haloacid dehalogenase family with a putative protein-tyrosine phosphatase function. Human recombinant MDP-1 acted on protein-bound fructosamine 6-phosphates with a catalytic efficiency > 10-fold higher than those observed with its next best substrates (arabinose 5-phosphate and free fructoselysine 6-phosphate) and > 100-fold higher than with protein-phosphotyrosine. It had no detectable activity on fructosamine 3-phosphates. MDP-1 dephosphorylated up to similar to 75% of the fructosamine 6-phosphates that are present on lysozyme after incubation of this protein with Glu-6-P. Furthermore, lysozyme glycated with Glu-6-P was converted by MDP-1 to a substrate for FN3K. We conclude that MDP-1 may act physiologically in conjunction with FN3K to free proteins from the glycation products derived from Glu-6-P.