2-formyl-3-(2-methoxycarbonylethyl)-4,5-dimethylpyrrole | 99986-60-4

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: 2-formyl-3-(2-methoxycarbonylethyl)-4,5-dimethylpyrrole
• 英文别名: methyl 3-(2-formyl-4,5-dimethyl-1H-pyrrol-3-yl)propanoate
• CAS: 99986-60-4
• 化学式: C₁₁H₁₅NO₃
• 分子量: 209.245
• InChiKey: RUXLBRDZDYLSAQ-UHFFFAOYSA-N

物化性质

• 熔点：
  91-93 °C
• 沸点：
  335.0±37.0 °C(Predicted)
• 密度：
  1.154±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  15
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.45
• 拓扑面积：
  59.2
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  2-formyl-3-(2-methoxycarbonylethyl)-4,5-dimethylpyrrole 在 氢溴酸 、 溶剂黄146 、 copper dichloride 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 6.57h， 生成 2,7-di(2-methoxycarbonylethyl)-3,8,12,17-tetramethyl-13,18-divinylporphyrin
  参考文献：
  名称：

  Smith, Kevin M.; Pandey, Ravindra K., Journal of Heterocyclic Chemistry, 1985, vol. 22, p. 1041 - 1044

  摘要：

  DOI：
• 作为产物：
  描述：

  benzyl 3-(2-methoxycarbonylethyl)-4,5-dimethylpyrrole-2-carboxylate 在 palladium 10% on activated carbon 、 氢气 、 三乙胺 、 三氟乙酸 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 18.83h， 生成 2-formyl-3-(2-methoxycarbonylethyl)-4,5-dimethylpyrrole
  参考文献：
  名称：

  Investigations regarding the utility of prodigiosenes to treat leukemia

  摘要：

  灵菌烯具有 4-甲氧基吡咯基二吡林骨架，以其抗癌活性而闻名。 C 环的结构修饰产生了一系列灵菌烯，在针对 NCI 60 癌细胞系组的体外分析中，这些灵菌烯显示出针对白血病细胞系的有希望的活性。使用斑马鱼模型对这些化合物进行的进一步体内研究表明，在人类 K562 慢性粒细胞白血病细胞中具有持久的抗白血病特性。

  DOI：

  10.1039/c2ob26535d

文献信息

• Synthetic and biosynthetic studies of porphyrins. Part 8. Syntheses of hepta-, hexa-, and penta-carboxylic porphyrins related to uroporphyrin-I
  作者：Anthony H. Jackson、Damrus Supphayen

  DOI：10.1039/p19870000277

  日期：——

  The title porphyrins, of interest as abnormal metabolites in porphyrin biosynthesis, have been synthesized by the Fischer, and b-oxobilane routes, and compared with the naturally derived materials. Enzymic experiments have shown that the conversion of uroporphyrinogen-I into coproporphyrinogen-I both in vivo and in vitro is non-specific and occurs by both possible pathways via the two intermediate

  标题卟啉，作为卟啉生物合成中的异常代谢产物，已经通过费歇尔和b-氧杂环丁烷路线合成，并与天然物质进行了比较。酶学实验表明，尿卟啉原-I在体内和体外的转化都是非特异性的，并且通过两种中间的六羧酸卟啉原通过两种可能的途径发生。
• Normal and Abnormal Heme Biosynthesis. 6. Synthesis and Metabolism of a Series of Monovinylporphyrinogens Related to Harderoporphyrinogen. Further Insights into the Oxidative Decarboxylation of Porphyrinogen Substrates by Coproporphyrinogen Oxidase
  作者：Timothy D. Lash、Ukti N. Mani、Anna-Sigrid I. M. Keck、Marjorie A. Jones

  DOI：10.1021/jo100083t

  日期：2010.5.21

  A series of vinylporphyrinogens were prepared to probe the enzyme coproporphyrinogen oxidase (CPO). Six (2-chloroethyl)porphyrins were synthesized from a common dipyrrylmethane via a,c-biladiene intermediates in excellent yields. Subsequent dehydrohalogenation with DBU in refluxing DMF then gave the required vinylporphyrin methyl esters, including harderoporphyrin-I, harderoporphyrin-III, and isoharderoporphyrin

  制备了一系列乙烯基卟啉原，以探测酶原卟啉原氧化酶（CPO）。从常见的二吡咯甲烷经a，c合成六种（2-氯乙基）卟啉-biladiene中间体，产率极高。随后在回流的DMF中用DBU进行脱卤化氢，得到所需的乙烯基卟啉甲酯，包括硬卟啉-I，硬卟啉-III和异硬卟啉。将相应的卟啉原羧酸与含有CPO酶的鸡红细胞裂解液一起孵育，并分析产物。硬质卟啉原III的17-乙基类似物，而不是其13-乙基异构体，被证明是CPO的优良底物，符合该酶活性位点的拟议模型。另外，显示出硬卟啉原-VII，即协同原卟啉原-IV代谢中的单乙烯基中间体，是该酶的同样良好的底物。但是，异硬质卟啉原缺乏外围取代基的正确顺序，也是CPO的底物。此外，显示出硬质卟啉原的非天然I型异构体可被CPO作用，但在这种情况下，可观察到进一步的代谢，从而提供了前所未有的三乙烯基卟啉原产物。分离出相应的卟啉甲酯，并通过FAB MS和质子NMR光谱进行
• Unprecedented overmetabolism of a porphyrinogen substrate by coproporphyrinogen oxidase
  作者：Timothy D. Lash、Anna-Sigrid I.M. Keck、Ukti N. Mani、Marjorie A. Jones

  DOI：10.1016/s0960-894x(02)00097-5

  日期：2002.4

  Harderoporphyrinogen-I is metabolized by avian hemolysate preparations of coproporphyrinogen oxidase to give a trivinylic product; this unprecedented 'overmetabolism' of the porphyrinogen substrate provides strong support for a proposed model of the active site of this poorly understood enzyme.

  Harderoporphyrinogen-I被原卟啉原氧化酶的禽血裂解物制剂代谢，得到三乙烯基产物；卟啉原底物的这种前所未有的“过度代谢”为这种鲜为人知的酶的活性位点的拟议模型提供了有力的支持。
• Normal and Abnormal Heme Biosynthesis. 1. Synthesis and Metabolism of Di- and Monocarboxylic Porphyrinogens Related to Coproporphyrinogen-III and Harderoporphyrinogen:  A Model for the Active Site of Coproporphyrinogen Oxidase
  作者：Timothy D. Lash、Ukti N. Mani、Martin A. Drinan、Chun Zhen、Troii Hall、Marjorie A. Jones

  DOI：10.1021/jo981473f

  日期：1999.1.1

  Coproporphyrinogen oxidase (copro'gen oxidase), which catalyses the conversion of coproporphyrinogen-III via a monovinylic intermediate to protoporphyrinogen-IX, is one of the least well understood enzymes in the heme biosynthetic pathway. To develop a model for the substrate recognition and binding recognition for this enzyme, a series of substrate analogues were prepared with two alkyl substituents on positions 13 and 17 in place of the usual propionate residues. Although the required substrate probes are porphyrinogens (hexahydroporphyrins), the corresponding porphyrin methyl esters were initialy synthesized via a,c-biladiene intermediates. These were hydrolyzed and reduced with 3% sodium amalgam to give the unstable porphyrinogens needed for the biochemical investigations. These modified structures were metabolized by avian preparations of copro'gen oxidase to give monovinylic products, but the second propionate residue was not further metabolized. In three cases, the metabolites were isolated and further characterized by proton NMR spectroscopy and mass spectrometry. When methyl or ethyl groups were placed at the 13 and 17 positions, the resulting porphyrinogens were very good substrates (although the ethyl version, mesoporphyrinogen-VI, gave slightly better results), but when propyl units were introduced metabolism was significantly inhibited and the butyl-substituted structure was only slightly transformed after long incubation periods. These results suggest the presence of an active-site lipophobic region near the catalytic site for copro'gen oxidase. The observation that the related 3-vinyl- and 3-ethylporphyrinogens with 13,17-diethyl substituents were not substrates for this enzyme confirmed the need for a second propionate residue to hold the substrate in place at the catalytic site.
• Normal and Abnormal Heme Biosynthesis. 2.¹ Synthesis and Metabolism of Type-III Pentacarboxylic Porphyrinogens:  Further Experimental Evidence for the Enzymic Clockwise Decarboxylation of Uroporphyrinogen-III
  作者：Timothy D. Lash、Ukti N. Mani、Elizabeth A. Lyons、Pornlert Thientanavanich、Marjorie A. Jones

  DOI：10.1021/jo9814748

  日期：1999.1.1

  Uroporphyrinogen decarboxylase catalyses the sequential decarboxylation of uroporphyrinogen-III (1) to-give coproporphyrinogen-III (2), a precursor to the hemes and chlorophylls. This involves the decarboxylation of four nonequivalent acetate side chains to produce methyl units and in principle could take place by 24 different pathways involving up to 14 intermediary porphyrinogens. In the past, seemingly contradictory data have been presented that either support an ordered "clockwise" decarboxylation pathway or a random decarboxylation process. Four pentacarboxylate porphyrinogens might be involved immediately before the formation of 2, and these compounds have been synthesized as the corresponding porphyrin pentamethyl esters via tripyrrene and a,c-biladiene intermediates. Hydrolysis of the methyl esters and reduction with 3% sodium amalgam gave the required porphyrinogens, and these were incubated with crude enzyme preparations derived from chicken red cell hemolysates. One of these pentacarboxylate porphyrinogens (5dab) consistently proved to be a much better substrate than the other three, providing new support for the "clockwise" pathway for coproporphyrinogen-III formation.