5-ethyl-dihydro-furan-2,3-dione | 2408-25-5

• 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: 5-ethyl-dihydro-furan-2,3-dione
• 英文别名: 5-Aethyl-dihydro-furan-2,3-dion；2-Oxo-4-ethyl-butyrolacton；2-Oxo-4-ethylbutyrolactone；5-ethyloxolane-2,3-dione
• CAS: 2408-25-5
• 化学式: C₆H₈O₃
• 分子量: 128.128
• InChiKey: NGEABPIXROYXEY-UHFFFAOYSA-N

物化性质

• 熔点：
  43-45 °C
• 沸点：
  284.6±7.0 °C(Predicted)
• 密度：
  1.161±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  9
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  43.4
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  4-hydroxy-2-oxohexanoic acid 在 盐酸 作用下， 生成 5-ethyl-dihydro-furan-2,3-dione
  参考文献：
  名称：

  Comparison of Two Metal-Dependent Pyruvate Aldolases Related by Convergent Evolution: Substrate Specificity, Kinetic Mechanism, and Substrate Channeling

  摘要：

  HpaI and BphI are two pyruvate class II aldolases found in aromatic meta-cleavage degradation pathways that catalyze similar reactions but are not related in sequence. Steady-state kinetic analysis of the aldol addition reactions and product inhibition assays showed that HpaI exhibits a rapid equilibrium random order mechanism while BphI exhibits a compulsory order mechanism, with pyruvate binding first. Both aldolases are able to utilize aldehyde acceptors two to five carbons in length; however, HpaI showed broader specificity and had a preference for aldehydes containing longer linear alkyl chains or C2-OH substitutions. Both enzymes were able to bind 2-keto acids larger than pyruvate, but only HpaI was able to utilize both pyruvate and 2-ketobutanoate as carbonyl donors in the aldol addition reaction. HpaI lacks stereospecific control producing racemic mixtures of 4-hydroxy-2-oxopentanoate (HOPA) from pyruvate and acetaldehyde while BphI synthesizes only (4S)-HOPA. BphI is also able to utilize acetaldehyde produced by the reduction of acetyl-CoA catalyzed by the associated aldehyde dehydrogenase, BphJ. This aldehyde was directly channeled from the dehydrogenase to the aldolase active sites, with an efficiency of 84%. Furthermore, the BphJ reductive deacylation reaction increased 4-fold when BphI was catalyzing the aldol addition reaction. Therefore, the BphI-BphJ enzyme complex exhibits unique bidirectionality in substrate channeling and allosteric activation.

  DOI：

  10.1021/bi100251u

文献信息

• Alcuni ?-cheto-?-lattoni con sostituenti alchilici in posizione ?
  作者：A. Rossi、H. Schinz

  DOI：10.1002/hlca.19480310226

  日期：——

  Durch Kondensation von Natrium-oxalessigester rnit aliphatischen Aldehyden gelangt man xu α-Keto-β-carboxathyl-γ-alkyl-γ-lactonen (A)

  草酰乙酸钠与脂肪族醛的缩合导致生成xα-酮基-β-羧基-γ-烷基-γ-内酯（A）
• Chorlin; Priwalowa, Khimiia Prirodnykh Soedineniĭ, 1967, p. 191,196
  作者：Chorlin、Priwalowa

  DOI：——

  日期：——
• Comparison of Two Metal-Dependent Pyruvate Aldolases Related by Convergent Evolution: Substrate Specificity, Kinetic Mechanism, and Substrate Channeling
  作者：Weijun Wang、Perrin Baker、Stephen Y. K. Seah

  DOI：10.1021/bi100251u

  日期：2010.5.4

  HpaI and BphI are two pyruvate class II aldolases found in aromatic meta-cleavage degradation pathways that catalyze similar reactions but are not related in sequence. Steady-state kinetic analysis of the aldol addition reactions and product inhibition assays showed that HpaI exhibits a rapid equilibrium random order mechanism while BphI exhibits a compulsory order mechanism, with pyruvate binding first. Both aldolases are able to utilize aldehyde acceptors two to five carbons in length; however, HpaI showed broader specificity and had a preference for aldehydes containing longer linear alkyl chains or C2-OH substitutions. Both enzymes were able to bind 2-keto acids larger than pyruvate, but only HpaI was able to utilize both pyruvate and 2-ketobutanoate as carbonyl donors in the aldol addition reaction. HpaI lacks stereospecific control producing racemic mixtures of 4-hydroxy-2-oxopentanoate (HOPA) from pyruvate and acetaldehyde while BphI synthesizes only (4S)-HOPA. BphI is also able to utilize acetaldehyde produced by the reduction of acetyl-CoA catalyzed by the associated aldehyde dehydrogenase, BphJ. This aldehyde was directly channeled from the dehydrogenase to the aldolase active sites, with an efficiency of 84%. Furthermore, the BphJ reductive deacylation reaction increased 4-fold when BphI was catalyzing the aldol addition reaction. Therefore, the BphI-BphJ enzyme complex exhibits unique bidirectionality in substrate channeling and allosteric activation.