D-saccharate | 5785-59-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: D-saccharate
• 英文别名: d-glucarate；saccharate；Saccharat；glucarate；(2S,3S,4S,5R)-2,3,4,5-tetrahydroxyhexanedioate
• CAS: 5785-59-1
• 化学式: C₆H₈O₈
• 分子量: 208.125
• InChiKey: DSLZVSRJTYRBFB-LLEIAEIESA-L

计算性质

• 辛醇/水分配系数(LogP)：
  -1.8
• 重原子数：
  14
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  161
• 氢给体数：
  4
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  D-saccharate 在 potassium phosphate 、 glucarate dehydratase from Pseudomonas putida 、 magnesium chloride 作用下， 以 水 为溶剂， 生成
  参考文献：
  名称：

  Importance of Mechanistic Imperatives in Enzyme-Catalyzed β-Elimination Reactions:  Stereochemical Consequences of the Dehydration Reactions Catalyzed by d-Galactonate Dehydratase from Escherichia coli and d-Glucarate Dehydratase from Pseudomonas putida

  摘要：

  DOI：

  10.1021/ja970977c
• 作为产物：
  描述：

  L-idarate 生成 D-saccharate
  参考文献：
  名称：

  Evolution of Enzymatic Activities in the Enolase Superfamily:  Characterization of the (D)-Glucarate/Galactarate Catabolic Pathway in Escherichia coli

  摘要：

  The genes encoding the enzymes in the (D)-glucarate/galactarate catabolic pathway have been identified in the Escherichia coli genome. These encode, in three transcriptional units, (D)-glucarate dehydratase (GlucD), galactarate dehydratase, 5-keto-4-deoxy-(D)-glucarate aldolase, tartronate semialdehyde reductase, a glycerate kinase that generates 2-phosphoglycerate as product, and two hexaric acid transporters. We also have identified a gene proximal to that encoding GlucD that encodes a protein that is 72% identical in primary sequence to GlucD (GlucD-related protein or GlucDRP). However, whereas GlucD catalyzes the efficient dehydration of both (D)-glucarate and (L)-idarate as well as their epimerization, GlucDRP is significantly impaired in both reactions. Perhaps GlucDRP is an example of gene duplication and evolution in progress in the E. coli chromosome.

  DOI：

  10.1021/bi981124f

文献信息

• 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。
• Enzymic Synthesis of Caffeoylglucaric Acid from Chlorogenic Acid and Glucaric Acid by a Protein Preparation from Tomato Cotyledons
  作者：Dieter Strack、Wiltrud Gross、Victor Wray、Lutz Grotjahn

  DOI：10.1104/pp.83.3.475

  日期：1987.3.1

  The phenylpropane metabolism of tomato (Lycopersicon esculentum Mill) cotyledons was investigated. The HPLC analysis revealed two hydroxycinnamic-acid conjugates as major components, identified as chlorogenic acid (5-O-caffeoylquinic acid) and caffeoylglucaric acid (2-O- or 5-O-caffeoyl-glucaric acid). Quantitative analyses indicated a precursor-product relationship between the chlorogenic and caffeoylglucaric acids. Protein preparations from tomato cotyledons were found to catalyze the formation of caffeoylglucaric acid with chlorogenic acid as acyl donor and free glucaric acid as acceptor molecule. This enzyme activity, possibly to be classified as hydroxycinnamoylquinic acid:glucaric acid hydroxycinnamoyltransferase, acts together with hydroxycinnamoyl-CoA: quinic acid hydroxycinnamoyltransferase.

  对番茄（Lycopersicon esculentum Mill）子叶的苯丙烷代谢进行了研究。HPLC分析显示，两种羟基肉桂酸结合物为主要成分，分别为绿原酸（5-O-咖啡酰奎尼酸）和咖啡酰葡萄糖酸（2-O-或5-O-咖啡酰葡萄糖酸）。定量分析表明，绿原酸和咖啡酰葡萄糖酸之间存在前体-产物关系。研究发现，番茄子叶中的蛋白质制剂可催化咖啡酰葡萄糖酸的形成，其中绿原酸为酰基供体，游离葡萄糖酸为受体分子。这种酶活性可能属于羟基肉桂酰奎尼酸：葡萄糖酸羟基肉桂酰转移酶，与羟基肉桂酰-CoA：奎尼酸羟基肉桂酰转移酶共同作用。
• Properties and Activity Changes of Chlorogenic Acid:Glucaric Acid Caffeoyltransferase From Tomato (<i>Lycopersicon esculentum</i>)
  作者：Dieter Strack、Wiltrud Gross

  DOI：10.1104/pp.92.1.41

  日期：1990.1.1

  A novel acyltransferase from cotyledons of tomato (Lycopersicon esculentum Mill.), which catalyzes the transfer of caffeic acid from chlorogenic acid (5-O-caffeoylquinic acid) to glucaric and galactaric acids, was purified with a 2400-fold enrichment and a 4% recovery. The enzyme showed specific activities (theoretical V  max per milligram of protein) of 625 nanokatals (caffeoylglucaric acid formation) and 310 nanokatals (caffeoylgalactaric acid formation). On sodium dodecyl sulfate-polyacrylamide gel electrophoresis it gave an apparent M  r of 40,000, identical to the value obtained by gel filtration column chromatography. Highest activity was found at pH 5.7, which was constant over a range of 20 to 120 millimolar K-phosphate. The isoelectric point of the enzyme was at pH 5.75. The reaction temperature optimum was at 38°C and the apparent energy of activation was calculated to be 57 kilojoules per mole. The apparent K  m values were 0.4 millimolar for glucaric acid, 1.7 millimolar for galactaric acid, and with both acceptors as second substrates 20 millimolar for chlorogenic acid. The relative ratio of the V  max/K  m values for glucaric acid and galactaric acid was found to be 100:12. Substrate-competition experiments support the conclusion that one single enzyme is responsible for both the glucaric and galactaric acid ester formation with marked preference for glucaric acid. It is proposed that the enzyme be called chlorogenic acid:glucaric acid O-caffeoyltransferase (EC 2.3.1.-). The three caffeic acid-dependent enzyme activities involved in the formation of the glucaric and galactaric acid esters, the chlorogenic acid:glucaric acid caffeoyltransferase as the key activity as well as the caffeic acid:CoA ligase and the caffeoyl-CoA:quinic acid caffeoyltransferase as the preceding activities, were determined. The time course of changes in these activities were followed during development of the seedling in the cotyledons and growth of the young plant in the first and second leaf. The results from tomato seedlings suggest a sequential appearance of these enzymes.

  oform（三氯甲烷）和氯仿（chloroform）是两种不同的有机溶剂，前者是易燃的，后者是易挥发的。
• Besson; Fleche; Fuertes, Recueil des Travaux Chimiques des Pays-Bas, 1996, vol. 115, # 4, p. 217 - 221
  作者：Besson、Fleche、Fuertes、Gallezot、Lahmer

  DOI：——

  日期：——
• Schinschel, Carsten; Simon, Helmut, Angewandte Chemie, 1993, vol. 105, # 8, p. 1221 - 1223
  作者：Schinschel, Carsten、Simon, Helmut

  DOI：——

  日期：——