D-glucuronic acid 1-phosphate | 10345-04-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: D-glucuronic acid 1-phosphate
• 英文别名: (2S,3S,4S,5R)-3,4,5-trihydroxy-6-phosphonooxyoxane-2-carboxylic acid
• CAS: 10345-04-7
• 化学式: C₆H₁₁O₁₀P
• 分子量: 274.121
• InChiKey: AIQDYKMWENWVQJ-AQKNRBDQSA-N

物化性质

• 沸点：
  685.1±65.0 °C(Predicted)
• 密度：
  2.05±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -3.4
• 重原子数：
  17
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  174
• 氢给体数：
  6
• 氢受体数：
  10

反应信息

• 作为反应物：
  描述：

  D-glucuronic acid 1-phosphate 、 尿苷-5'-三磷酸 在 Pisum sativum UDP-sugar pyrophosphorylase 作用下， 生成 UDP-glucuronic acid
  参考文献：
  名称：

  Cloning of Glucuronokinase from Arabidopsis thaliana, the Last Missing Enzyme of the myo-Inositol Oxygenase Pathway to Nucleotide Sugars

  摘要：

  Nucleotide sugars are building blocks for carbohydrate polymers in plant cell walls. They are synthesized from sugar-1-phosphates or epimerized as nucleotide sugars. The main precursor for primary cell walls is UDP-glucuronic acid, which can be synthesized via two independent pathways. One starts with the ring cleavage of myo-inositol into glucuronic acid, which requires a glucuronokinase and a pyrophosphorylase for activation into UDP-glucuronate. Here we report on the purification of glucuronokinase from Lilium pollen. A 40-kDa protein was purified combining six chromatographic steps and peptides were de novo sequenced. This allowed the cloning of the gene from Arabidopsis thaliana and the expression of the recombinant protein in Escherichia coli for biochemical characterization. Glucuronokinase is a novel member of the GHMP-kinase superfamily having an unique substrate specificity for D-glucuronic acid with a K-m of 0.7 mM. It requires ATP as phosphate donor (K-m 0.56 mM). In Arabidopsis, the gene is expressed in all plant tissues with a preference for pollen. Genes for glucuronokinase are present in (all) plants, some algae, and a few bacteria as well as in some lower animals.

  DOI：

  10.1074/jbc.m109.069369
• 作为产物：
  描述：

  D-葡萄糖醛酸 、 5’-三磷酸腺苷 在 pyruvate kinase 、 磷烯醇丙酮酸 、 recombinant full-length Arabidopsis thaliana glucuronokinase At₃g01640 isoform (362 amino acids) 、 potassium chloride 、 还原型辅酶Ⅰ 、 magnesium chloride 、 L-lactate dehydrogenase 作用下， 反应 0.25h， 生成 D-glucuronic acid 1-phosphate 、 二磷酸腺苷
  参考文献：
  名称：

  Cloning of Glucuronokinase from Arabidopsis thaliana, the Last Missing Enzyme of the myo-Inositol Oxygenase Pathway to Nucleotide Sugars

  摘要：

  Nucleotide sugars are building blocks for carbohydrate polymers in plant cell walls. They are synthesized from sugar-1-phosphates or epimerized as nucleotide sugars. The main precursor for primary cell walls is UDP-glucuronic acid, which can be synthesized via two independent pathways. One starts with the ring cleavage of myo-inositol into glucuronic acid, which requires a glucuronokinase and a pyrophosphorylase for activation into UDP-glucuronate. Here we report on the purification of glucuronokinase from Lilium pollen. A 40-kDa protein was purified combining six chromatographic steps and peptides were de novo sequenced. This allowed the cloning of the gene from Arabidopsis thaliana and the expression of the recombinant protein in Escherichia coli for biochemical characterization. Glucuronokinase is a novel member of the GHMP-kinase superfamily having an unique substrate specificity for D-glucuronic acid with a K-m of 0.7 mM. It requires ATP as phosphate donor (K-m 0.56 mM). In Arabidopsis, the gene is expressed in all plant tissues with a preference for pollen. Genes for glucuronokinase are present in (all) plants, some algae, and a few bacteria as well as in some lower animals.

  DOI：

  10.1074/jbc.m109.069369

文献信息

• PROCESS FOR SELECTIVE OXIDATION OF PRIMARY ALCOHOLS
  申请人：Nederlandse Organisatie voor Toegepast Natuurwetenschappelijk Onderzoek TNO

  公开号：EP1093467A1

  公开（公告）日：2001-04-25
• [EN] PROCESS FOR SELECTIVE OXIDATION OF PRIMARY ALCOHOLS<br/>[FR] PROCEDE PERMETTANT D'OXYDER SELECTIVEMENT LES ALCOOLS PRIMAIRES
  申请人：NEDERLANDSE ORGANISATIE VOOR TOEGEPAST NATUURWETENSCHAPPELIJK ONDERZOEK TNO

  公开号：WO1999057158A1

  公开（公告）日：1999-11-11

  (EN) Primary alcohols, especially in carbohydrates, can be selectively oxidised to aldehydes and carboxylic acids in a low-halogen process by using a peracid in the presence of a catalytic amount of a di-tertiary-alkyl nitroxyl (TEMPO) and a catalytic amount of halide. The halide is preferably bromide and the process can be carried out at nearly neutral to moderately alkaline pH (5-11). The peracid can be produced or regenerated by means of hydrogen peroxide or oxygen. The process is advantageous for producing uronic acids and for introducing aldehyde groups which are suitable for crosslinking and derivatisation.(FR) Les alcools primaires, notamment ceux contenus dans les glucides, peuvent être sélectivement oxydés en aldéhydes et acides carboxyliques par un procédé faiblement halogéné utilisant un peracide, en présence d'une quantité catalytique d'un alkyl-nitroxyle di-tertiaire (TEMPO) et d'une quantité catalytique d'halogénure. Ce dernier est de préférence le bromure et le procédé peut être mis en oeuvre à un pH pratiquement neutre ou modérément alcalin (5-11). Le peracide peut être produit ou régénéré au moyen de peroxyde d'hydrogène ou d'oxygène. Ce procédé est avantageux pour produire des acides uroniques et introduire des groupes aldéhyde permettant la réticulation et la dérivatisation.
• Cloning of Glucuronokinase from Arabidopsis thaliana, the Last Missing Enzyme of the myo-Inositol Oxygenase Pathway to Nucleotide Sugars
  作者：Anja Maria Pieslinger、Marion Christine Hoepflinger、Raimund Tenhaken

  DOI：10.1074/jbc.m109.069369

  日期：2010.1

  Nucleotide sugars are building blocks for carbohydrate polymers in plant cell walls. They are synthesized from sugar-1-phosphates or epimerized as nucleotide sugars. The main precursor for primary cell walls is UDP-glucuronic acid, which can be synthesized via two independent pathways. One starts with the ring cleavage of myo-inositol into glucuronic acid, which requires a glucuronokinase and a pyrophosphorylase for activation into UDP-glucuronate. Here we report on the purification of glucuronokinase from Lilium pollen. A 40-kDa protein was purified combining six chromatographic steps and peptides were de novo sequenced. This allowed the cloning of the gene from Arabidopsis thaliana and the expression of the recombinant protein in Escherichia coli for biochemical characterization. Glucuronokinase is a novel member of the GHMP-kinase superfamily having an unique substrate specificity for D-glucuronic acid with a K-m of 0.7 mM. It requires ATP as phosphate donor (K-m 0.56 mM). In Arabidopsis, the gene is expressed in all plant tissues with a preference for pollen. Genes for glucuronokinase are present in (all) plants, some algae, and a few bacteria as well as in some lower animals.