2-Oxo-δ-caprolacton | 100191-40-0

• 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: 2-Oxo-δ-caprolacton
• 英文别名: 6-methyl-dihydro-pyran-2,3-dione；Dihydro-6-methyl-2H-pyran-2,3(4H)-dione；6-methyloxane-2,3-dione
• CAS: 100191-40-0
• 化学式: C₆H₈O₃
• 分子量: 128.128
• InChiKey: CXPFNERGELIGPL-UHFFFAOYSA-N

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：
  0.67
• 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：

  5-Hydroxy-2-oxohexanoic acid 在 盐酸 作用下， 生成 2-Oxo-δ-caprolacton
  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

• Composition à base d'alpha-pyrones pour induire et stimuler la croissance des cheveux et/ou freiner leur chute et utilisation
  申请人：L'OREAL

  公开号：EP0672406A1

  公开（公告）日：1995-09-20

  L'invention concerne une composition cosmétique et/ou thérapeutique à usage topique destinée à induire et stimuler la croissance des cheveux et/ou à diminuer leur chute, qui est caractérisé par le fait qu'elle comprend, dans un milieu physiologiquement acceptable, au moins une α-Pyrone. Elle concerne également l'utilisation d'une telle composition dans le traitement cosmétique et/ou thérapeutique, par voie topique, de la chute ou de la pousse des cheveux.

  本发明涉及一种用于外用的化妆品和/或治疗组合物，旨在诱导和刺激头发生长和/或减少脱发，其特征在于它在生理上可接受的介质中包含至少一种α-吡喃酮。 它还涉及将这种组合物用于脱发或生发的局部美容和/或治疗。
• L'utilisation d'une composition à base d'alpha-pyrones pour induire et stimuler la croissance des cheveux et/ou freiner leur chute.
  申请人：L'OREAL

  公开号：EP0672406B1

  公开（公告）日：2000-02-16
• 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.