3-Succinoyl-6-pyridon | 15873-27-5

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 酮酸及其衍生物
• 英文名称: 3-Succinoyl-6-pyridon
• 英文别名: 4-(6-Hydroxypyridin-3-yl)-4-oxobutyric acid；4-oxo-4-(6-oxo-1H-pyridin-3-yl)butanoic acid
• CAS: 15873-27-5
• 化学式: C₉H₉NO₄
• 分子量: 195.175
• InChiKey: OMAJIMAYOJBLJF-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1
• 重原子数：
  14
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.22
• 拓扑面积：
  83.5
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  3-Succinoyl-6-pyridon 在 氯 、 三氯氧磷 作用下， 以 甲醇 为溶剂， 反应 4.5h， 生成 methyl 4-(5,6-dichloropyridin-3-yl)-4-oxobutyrate
  参考文献：
  名称：

  Renewable Functionalized Pyridines Derived from Microbial Metabolites of the Alkaloid (S)-Nicotine

  摘要：

  DOI：

  10.3987/com-97-7827
• 作为产物：
  描述：

  烟碱 在 pseudomonas nicotinopharga 作用下， 生成 3-Succinoyl-6-pyridon
  参考文献：
  名称：

  Degradation of Nicotine by Soil Bacteria¹

  摘要：

  DOI：

  10.1021/ja01630a042

文献信息

• Wada, Archives of Biochemistry, 1957, vol. 72, p. 145,149, 1541
  作者：Wada

  DOI：——

  日期：——
• Tabuchi, Nippon Nogeikagaku Kaishi, 1955, vol. 29, p. 222,223
  作者：Tabuchi

  DOI：——

  日期：——
• Frankenburg; Vaitekunas, Archives of Biochemistry, 1955, vol. 58, p. 509,512
  作者：Frankenburg、Vaitekunas

  DOI：——

  日期：——
• Mechanism of the 6-Hydroxy-3-succinoyl-pyridine 3-Monooxygenase Flavoprotein from Pseudomonas putida S16
  作者：Hao Yu、浩 于、Robert P. Hausinger、Hong-Zhi Tang、鸿志 唐、Ping Xu、平 许

  DOI：10.1074/jbc.m114.558049

  日期：2014.10

  6-Hydroxy-3-succinoyl-pyridine (HSP) 3-monooxygenase (HspB), a flavoprotein essential to the pyrrolidine pathway of nicotine degradation, catalyzes pyridine-ring beta-hydroxylation, resulting in carbon-carbon cleavage and production of 2,5-dihydroxypyridine. Here, we generated His(6)-tagged HspB in Escherichia coli, characterized the properties of the recombinant enzyme, and investigated its mechanism of catalysis. In contrast to conclusions reported previously, the second product of the HspB reaction was shown to be succinate, with isotope labeling experiments providing direct evidence that the newly introduced oxygen atom of succinate is derived from H2O. Phylogenetic analysis reveals that HspB is the most closely related to two p-nitrophenol 4-monooxygenases, and the experimental results exhibit that p-nitrophenol is a substrate of HspB. The reduction of HspB (with maxima at 375 and 460 nm, and a shoulder at 485 nm) by NADH was followed by stopped-flow spectroscopy, and the rate constant for reduction was shown to be stimulated by HSP. Reduced HspB reacts with oxygen to form a C-(4a)-(hydro)peroxyflavin intermediate with an absorbance maximum at similar to 400 nm within the first few milliseconds before converting to the oxidized flavoenzyme species. The formed C-(4a)-hydroperoxyflavin intermediate reacts with HSP to form an intermediate that hydrolyzes to the products 2,5-dihydroxypyridine and succinate. The investigation on the catalytic mechanism of a flavoprotein pyridine-ring beta-position hydroxylase provides useful information for the biosynthesis of pyridine derivatives.
• US5760236A
  申请人：——

  公开号：US5760236A

  公开（公告）日：1998-06-02

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