(2S)-5-oxooxolane-2-carboxylate | 21461-84-7

• 物质功能分类: 分析化学 - 分析试剂 - 常用分析试剂
• 分子结构分类: 有机化合物 - 有机杂环化合物 - 内酯类
• 英文名称: (2S)-5-oxooxolane-2-carboxylate
• CAS: 21461-84-7
• 化学式: C5H5O4-
• 分子量: 129.09
• InChiKey: QVADRSWDTZDDGR-VKHMYHEASA-M

物化性质

• 熔点：
  71-73 °C (lit.)
• 比旋光度：
  +14°(20/D, c=5, CH3OH)
• 沸点：
  150-155 °C/0.2 mmHg (lit.)
• 密度：
  1.3985 (rough estimate)
• 溶解度：
  溶于丙酮

计算性质

• 辛醇/水分配系数(LogP)：
  0.5
• 重原子数：
  9
• 可旋转键数：
  0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.6
• 拓扑面积：
  66.4
• 氢给体数：
  0
• 氢受体数：
  4

安全信息

• 危险品标志：
  Xi
• 安全说明：
  S26,S36
• 危险类别码：
  R36/37/38
• WGK Germany：
  3
• 海关编码：
  2932190090
• 危险性防范说明：
  P261,P305+P351+P338
• 危险性描述：
  H315,H319,H335

反应信息

• 作为反应物：
  描述：

  (2S)-5-oxooxolane-2-carboxylate 、 水 生成 (R)-2-hydroxyglutarate 、 氢(+1)阳离子
  参考文献：
  名称：

  Purification and characterization of a lactonase from Erwinia cypripedii 314B that hydrolyzes ( S )-5-oxo-2-tetrahydrofurancarboxylic acid

  摘要：

  A bacterium, strain 314B, able to assimilate (S)-5-oxo-2-tetrahydrofurancarboxylic acid was isolated from soil and identified as Erwinia cypripedii. A lactonase hydrolyzing (S)-5-oxo-2-tetrahydrofurancarboxylic acid to L-alpha-hydroxyglutaric acid was purified 63-fold with 2% recovery from crude extracts of this bacterium to homogeneity as judged by SDS-PAGE. The molecular masses estimated by SDS-PAGE and gel filtration were 41 kDa and 79 kDa, respectively. The maximum activity was observed at pH 6.5-7.5 and 35-45 degreesC. The enzyme showed lower activity toward DL-2-oxotetrahydrofuran-4,5-dicarboxylic acid, but did not act on (R)-5-oxo-2-tetrahydrofurancarboxylic acid and other natural and synthetic lactones tested.

  DOI：

  10.1007/s00203-003-0597-5

文献信息

• Cloning, sequencing, and heterologous expression of an Erwinia cypripedii 314B lactonase specific for l-α-hydroxyglutaric acid γ-lactone
  作者：Kazuya Mochizuki

  DOI：10.1007/s00253-005-0224-2

  日期：2006.8

  The gene for a lactonase that stereospecifically hydrolyzes (S)-5-oxo-2-tetrahydrofurancarboxylic acid to L-alpha-hydroxyglutaric acid was isolated from Erwinia cypripedii 314B. Determination of the nucleotide sequence showed that the gene consists of a single open reading frame of 1,152 by that encodes a 383-amino-acid protein. Comparison of the sequence of the predicted protein to that of the enzyme purified from E. cypripedii 314B revealed an N-terminal signal sequence of 19 amino acids. The gene for the mature enzyme was inserted into a pET vector and overexpressed in Escherichia coli. Active recombinant enzyme accumulated in the cells to similar to 30% of the total protein, and the enzyme was purified to homogeneity. The physical and catalytic properties of the recombinant enzyme were indistinguishable from those of the protein purified from E. cypripedii 314B. The deduced amino acid sequence displayed similar to 35% similarity with a putative 3-carboxymuconate cyclase, but exhibited no such activity. The enzyme also showed similar to 35% similarity with 6-phosphogluconolactonase. However, the activity of the enzyme toward 6-phosphogluconolactone was less than 2% of that toward (S)-5-oxo-2-tetrahydrofurancarboxylic acid, demonstrating a novel specificity for this lactonase.