L-idarate

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: L-idarate
• 英文别名: (2R,3S,4S,5R)-2,3,4,5-tetrahydroxyhexanedioate
• 化学式: C₆H₈O₈
• 分子量: 208.125
• InChiKey: DSLZVSRJTYRBFB-ORZLYADOSA-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：

  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

• Importance of Mechanistic Imperatives in Enzyme-Catalyzed β-Elimination Reactions:  Stereochemical Consequences of the Dehydration Reactions Catalyzed by <scp>d</scp>-Galactonate Dehydratase from <i>Escherichia coli </i>and <scp>d</scp>-Glucarate Dehydratase from <i>Pseudomonas putida</i>
  作者：David R. J. Palmer、Stacey J. Wieczorek、Brian K. Hubbard、Gregory T. Mrachko、John A. Gerlt

  DOI：10.1021/ja970977c

  日期：1997.10.1
• Evolution of Enzymatic Activities:  Multiple Pathways for Generating and Partitioning a Common Enolic Intermediate by Glucarate Dehydratase from <i>Pseudomonas putida</i>
  作者：David R. J. Palmer、John A. Gerlt

  DOI：10.1021/ja962126v

  日期：1996.1.1
• Duin, M. van; Peters, J. A.; Kieboom, A. P. G., Recueil des Travaux Chimiques des Pays-Bas, <hi>1986</hi>, vol. 105, p. 488 - 493
  作者：Duin, M. van、Peters, J. A.、Kieboom, A. P. G.、Bekkum, H. van

  DOI：——

  日期：——
• Evolution of Enzymatic Activities in the Enolase Superfamily:  Characterization of the (<i>D</i>)-Glucarate/Galactarate Catabolic Pathway in <i>Escherichia coli</i>
  作者：Brian K. Hubbard、Marjan Koch、David R. J. Palmer、Patricia C. Babbitt、John A. Gerlt

  DOI：10.1021/bi981124f

  日期：1998.10.1

  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.