D-glucuronate | 148-00-5

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: D-glucuronate
• 英文别名: glucuronate；D-Glucopyranuronic acid, ion(1-)；(2S,3S,4S,5R)-3,4,5,6-tetrahydroxyoxane-2-carboxylate
• CAS: 148-00-5
• 化学式: C₆H₉O₇
• 分子量: 193.133
• InChiKey: AEMOLEFTQBMNLQ-AQKNRBDQSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -1.7
• 重原子数：
  13
• 可旋转键数：
  0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  130
• 氢给体数：
  4
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  D-glucuronate 生成 D-fructofuranuronate
  参考文献：
  名称：

  ASHWELL G.; WAHBA A.J.; HICKMAN J., J Biol Chem, 1960, 0021-9258, 1559-65

  摘要：

  DOI：
• 作为产物：
  描述：

  a β-D-glucuronoside 、 水 生成 an alcohol 、 D-glucuronate
  参考文献：
  名称：

  DOYLE M.L.; KATZMAN P.A.; DOISY E.A., J Biol Chem, 1955, 0021-9258, 921-30

  摘要：

  DOI：

文献信息

• Crystal structure of a substrate complex of <i>myo</i> -inositol oxygenase, a di-iron oxygenase with a key role in inositol metabolism
  作者：Peter M. Brown、Tom T. Caradoc-Davies、James M. J. Dickson、Garth J. S. Cooper、Kerry M. Loomes、Edward N. Baker

  DOI：10.1073/pnas.0605143103

  日期：2006.10.10

  Altered metabolism of the inositol sugars myo -inositol (MI) and d - chiro -inositol is implicated in diabetic complications. In animals, catabolism of MI and d - chiro -inositol depends on the enzyme MI oxygenase (MIOX), which catalyzes the first committed step of the glucuronate–xylulose pathway, and is found almost exclusively in the kidneys. The crystal structure of MIOX, in complex with MI, has been determined by multiwavelength anomalous diffraction methods and refined at 2.0-Å resolution ( R = 0.206, R _free = 0.253). The structure reveals a monomeric, single-domain protein with a mostly helical fold that is distantly related to the diverse HD domain superfamily. Five helices form the structural core and provide six ligands (four His and two Asp) for the di-iron center, in which the two iron atoms are bridged by a putative hydroxide ion and one of the Asp ligands, Asp-124. A key loop forms a lid over the MI substrate, which is coordinated in bidentate mode to one iron atom. It is proposed that this mode of iron coordination, and interaction with a key Lys residue, activate MI for bond cleavage. The structure also reveals the basis of substrate specificity and suggests routes for the development of specific MIOX inhibitors.

  改变肌醇糖的代谢，即肌醇（MI）和D-手性肌醇（DCI）的代谢异常与糖尿病并发症有关。在动物体内，MI和DCI的分解取决于MI氧化酶（MIOX）这一酶，在葡萄糖醛酸-木糖途径中催化第一步反应，几乎只存在于肾脏中。采用多波长异常衍射方法确定了与MI复合物的MIOX晶体结构，并在2.0-Å分辨率下进行了修正（R = 0.206，Rfree = 0.253）。该结构显示出一个单域蛋白质的单体，具有大多数螺旋折叠，与多样化的HD域超家族有一定的关联。五个螺旋形成结构核心，并为二铁中心提供六个配体（四个组氨酸和两个天冬氨酸），其中两个铁原子由一个假定的氢氧根离子和一个天冬氨酸配体（天冬氨酸-124）桥接。一个关键的环形成MI底物的盖子，MI底物以双齿配位模式与一个铁原子配位。据推测，这种铁配位方式和与关键的赖氨酸残基的相互作用，激活MI进行键裂解。该结构还揭示了底物特异性的基础，并提出了特异性MIOX抑制剂的发展途径。
• Cloning and Characterization of Uronate Dehydrogenases from Two Pseudomonads and<i>Agrobacterium tumefaciens</i>Strain C58
  作者：Sang-Hwal Yoon、Tae Seok Moon、Pooya Iranpour、Amanda M. Lanza、Kristala Jones Prather

  DOI：10.1128/jb.00586-08

  日期：2009.3

  Uronate dehydrogenase has been cloned fromPseudomonas syringaepv. tomato strain DC3000,Pseudomonas putidaKT2440, andAgrobacterium tumefaciensstrain C58. The genes were identified by using a novel complementation assay employing anEscherichia colimutant incapable of consuming glucuronate as the sole carbon source but capable of growth on glucarate. A shotgun library ofP. syringaewas screened in the mutantE. coliby growing transformed cells on minimal medium containing glucuronic acid. Colonies that survived were evaluated for uronate dehydrogenase, which is capable of converting glucuronic acid to glucaric acid. In this manner, a 0.8-kb open reading frame was identified and subsequently verified to beudh. Homologous enzymes inP. putidaandA. tumefacienswere identified based on a similarity search of the sequenced genomes. Recombinant proteins from each of the three organisms expressed inE. coliwere purified and characterized. For all three enzymes, the turnover number (k_cat) with glucuronate as a substrate was higher than that with galacturonate; however, the Michaelis constant (K_m) for galacturonate was lower than that for glucuronate. TheA. tumefaciensenzyme was found to have the highest rate constant (k_cat= 1.9 × 10²s⁻¹on glucuronate), which was more than twofold higher than those of both of the pseudomonad enzymes.

  摘要 克隆了番茄假单胞菌（Pseudomonas syringaepv. tomato）菌株 DC3000、普特假单胞菌（Pseudomonas putidaKT2440）和农杆菌（Agrobacterium tumefaciens）菌株 C58 中的丙酮酸脱氢酶。这些基因是通过一种新的互补试验鉴定的，该试验采用了一种不能消耗葡萄糖醛酸作为唯一碳源但能在葡萄糖醛酸上生长的大肠埃希氏菌突变体。通过在含有葡萄糖醛酸的最小培养基上培养转化细胞，在突变体大肠埃希氏菌中筛选出了丁香球菌的射枪文库。对存活下来的菌落进行了尿酸脱氢酶评估，尿酸脱氢酶能够将葡萄糖醛酸转化为葡萄糖酸。通过这种方法，确定了一个 0.8 kb 的开放阅读框，并随后对其进行了验证。根据对已测序基因组的相似性检索，确定了普氏菌和肿瘤细胞中的同源酶。在大肠杆菌中表达的来自这三种生物的重组蛋白得到了纯化和鉴定。这三种酶以葡萄糖醛酸为底物时的转化率（kcat）均高于半乳糖醛酸；但半乳糖醛酸的迈克尔常数（Km）低于葡萄糖醛酸。发现A. tumefaci酶的速率常数最高（kcat= 1.9 × 102s-1），比两种假单胞菌酶的速率常数高出两倍多。
• Purification and Properties of a Plant .BETA.-D-Glucuronidase from Scutellaria Root.
  作者：Fumio IKEGAMI、Kaori MATSUNAE、Masafumi HISAMITSU、Takashi KURIHARA、Takeshi YAMAMOTO、Isamu MURAKOSHI

  DOI：10.1248/bpb.18.1531

  日期：——

  β-D-Glucuronidase (baicalinase, GUS [EC 3.2.1.31]) activity in the crude drug, Scutellaria root, was assayed in line with the quality control standards of Kampo (Japanese herbal) medicines. GUS was purified to homogeneity in the purification steps including DEAE-Sepharose Fast Flow and chromatofocusing used PBETM94 and Polybuffer 74. These results suggest that the Scutellaria GUS is composed of 55 kDa active subunits and that the isoelectric point of this enzyme is pH 5.4. Optimal catalytic activity was found at pH 4.7 in the pH range 3.6-6.2 in 50 mM Na-citrate buffer. The purified enzyme hydrolyzed baicalin and wogonin glucuronide, but did not hydrolyze glycyrrhizin or some β-glucosides found in other crude drugs. GUS activity in several crude drugs is also described.

  按照日本草药的质量控制标准，对粗制药物黄芩根中的β-D-葡糖醛酸酶（黄芩苷酶，GUS [EC 3.2.1.31]）活性进行了检测。在纯化步骤（包括 DEAE-Sepharose Fast Flow 和使用 PBETM94 和 Polybuffer 74 的色谱聚焦）中，GUS 被纯化至均一。这些结果表明，黄芩 GUS 由 55 kDa 的活性亚基组成，该酶的等电点为 pH 5.4。在 50 mM Na-citrate 缓冲液中，pH 值为 3.6-6.2 时，pH 值为 4.7 时催化活性最佳。纯化的酶水解黄芩苷和乌药苷葡萄糖醛酸，但不水解甘草苷或其他粗制药物中的一些β-葡萄糖苷。此外，还介绍了几种粗制药物中的 GUS 活性。
• Discovery and Functional Characterization of a Clandestine ATP-Dependent Amidoligase in the Biosynthesis of the Capsular Polysaccharide from <i>Campylobacter jejuni</i>
  作者：Alexander S. Riegert、Tamari Narindoshvili、Frank M. Raushel

  DOI：10.1021/acs.biochem.1c00707

  日期：2022.1.18

  unknown how this new amide bond is formed. Sequence similarity networks were used to identify a candidate enzyme for amide bond formation during the biosynthesis of the CPS of C. jejuni. The C-terminal domain of Cj1438 was shown to catalyze amide bond formation using MgATP and d-glucuronate in the presence of either ethanolamine phosphate or (S)-serinol phosphate. Product formation was verified using 31P

  空肠弯曲菌是一种革兰氏阴性致病菌，在家禽中是共生的。空肠弯曲杆菌感染导致弯曲杆菌病，这是全球胃肠炎的主要原因。包裹在空肠弯曲菌表面的是一层厚厚的糖分子，称为荚膜多糖 (CPS)。C. jejuni NCTC 11168 (HS:2)的 CPS由d -甘油- l -葡萄糖庚糖、d -葡萄糖醛酸盐、d - N -乙酰半乳糖胺和d-核糖。葡萄糖醛酸盐被乙醇胺或丝氨醇进一步酰胺化，但尚不清楚这种新的酰胺键是如何形成的。序列相似性网络用于鉴定空肠弯曲杆菌CPS 生物合成过程中形成酰胺键的候选酶。Cj1438 的 C 末端结构域显示在乙醇胺磷酸盐或 ( S )-丝氨醇磷酸盐存在的情况下使用 MgATP 和d-葡萄糖醛酸盐催化酰胺键形成。使用31验证产物形成P NMR 光谱和 ESI 质谱，以及通过测量 ADP 形成速率使用偶联酶测定法确定的动力学常数。这项工作代表了 ATP 依赖性酰胺寡聚酶在空肠弯曲菌中
• 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.