3,3,3-Tetraminium(4+)

• 分子结构分类: 有机化合物 - 有机氮化合物
• 英文名称: 3,3,3-Tetraminium(4+)
• 英文别名: 3-azaniumylpropyl-[3-(3-azaniumylpropylazaniumyl)propyl]azanium
• 化学式: C9H28N4+4
• 分子量: 192.35
• InChiKey: ZAXCZCOUDLENMH-UHFFFAOYSA-R

计算性质

• 辛醇/水分配系数(LogP)：
  -1.4
• 重原子数：
  13
• 可旋转键数：
  10
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  88.5
• 氢给体数：
  4
• 氢受体数：
  0

反应信息

• 作为反应物：
  描述：

  3,3,3-Tetraminium(4+) 、 S-Adenosyl-L-methioninamine 生成 Caldopentamine(4+) 、 氢(+1)阳离子 、 甲硫腺苷
  参考文献：
  名称：

  Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases fromHyperthermus butylicusandPyrobaculum aerophilum

  摘要：

  Polyamines are ubiquitously present in all organisms. In addition to the common polyamines, thermophilic archaea synthesize long‐chain polyamines. In the present study polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum were cloned and their substrate specificity was analyzed. The polyamine synthase HbSpeE II from H. butylicus synthesized long‐chain polyamines with high activity using the same mechanism that is used by a wide range of organisms to synthesize common polyamines, in which the aminopropyl residue derives from decarboxylated S‐adenosylmethionine. This is the first polyamine synthase described that synthesizes a polyamine longer than a tetramine with high activity.

  DOI：

  10.1016/j.febslet.2009.10.014
• 作为产物：
  描述：

  Bis(3-azaniumylpropyl)azanium 、 S-Adenosyl-L-methioninamine 生成 氢(+1)阳离子 、 3,3,3-Tetraminium(4+) 、 甲硫腺苷
  参考文献：
  名称：

  Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases fromHyperthermus butylicusandPyrobaculum aerophilum

  摘要：

  Polyamines are ubiquitously present in all organisms. In addition to the common polyamines, thermophilic archaea synthesize long‐chain polyamines. In the present study polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum were cloned and their substrate specificity was analyzed. The polyamine synthase HbSpeE II from H. butylicus synthesized long‐chain polyamines with high activity using the same mechanism that is used by a wide range of organisms to synthesize common polyamines, in which the aminopropyl residue derives from decarboxylated S‐adenosylmethionine. This is the first polyamine synthase described that synthesizes a polyamine longer than a tetramine with high activity.

  DOI：

  10.1016/j.febslet.2009.10.014

文献信息

• Heterologous Expression and Biochemical Characterization of a Polyamine Oxidase from Arabidopsis Involved in Polyamine Back Conversion
  作者：Paraskevi Tavladoraki、Marianna Nicoletta Rossi、Giuseppe Saccuti、Miguel Angel Perez-Amador、Fabio Polticelli、Riccardo Angelini、Rodolfo Federico

  DOI：10.1104/pp.106.080911

  日期：2006.8.1

  Polyamine oxidase (PAO) is a flavin adenine dinucleotide-dependent enzyme involved in polyamine catabolism. Animal PAOs oxidize spermine (Spm), spermidine (Spd), and/or their acetyl derivatives to produce H2O2, an aminoaldehyde, and Spd or putrescine, respectively, thus being involved in a polyamine back-conversion pathway. On the contrary, plant PAOs that have been characterized to date oxidize Spm and Spd to produce 1,3-diaminopropane, H2O2, and an aminoaldehyde and are therefore involved in the terminal catabolism of polyamines. A database search within the Arabidopsis (Arabidopsis thaliana) genome sequence showed the presence of a gene (AtPAO1) encoding for a putative PAO with 45% amino acid sequence identity with maize (Zea mays) PAO. The AtPAO1 cDNA was isolated and cloned in a vector for heterologous expression in Escherichia coli. The recombinant protein was purified by affinity chromatography on guazatine-Sepharose 4B and was shown to be a flavoprotein able to oxidize Spm, norspermine, and N1-acetylspermine with a pH optimum at 8.0. Analysis of the reaction products showed that AtPAO1 produces Spd from Spm and norspermidine from norspermine, demonstrating a substrate oxidation mode similar to that of animal PAOs. To our knowledge, AtPAO1 is the first plant PAO reported to be involved in a polyamine back-conversion pathway.

  多胺氧化酶（PAO）是一种依赖于黄素腺嘌呤二核苷酸的酶，参与多胺降解。动物PAOs氧化精胺（Spm）、亚精胺（Spd）和/或它们的乙酰衍生物，产生H2O2、氨基醛和Spd或腐胺，因此参与多胺回转途径。相反，到目前为止已经表征的植物PAOs氧化Spm和Spd，产生1,3-二氨基丙烷、H2O2和氨基醛，因此参与多胺的末端降解。在拟南芥（拟南芥）基因组序列中进行数据库搜索，显示存在一个编码推测PAO的基因（AtPAO1），其氨基酸序列同玉米（玉米）PAO具有45％的同源性。 AtPAO1 cDNA被分离并克隆到Escherichia coli的载体中进行异源表达。亲和层析在guazatine-Sepharose 4B上纯化重组蛋白，并显示为一种能够在pH 8.0下氧化Spm、norspermine和N1-acetylspermine的黄素蛋白。反应产物的分析表明，AtPAO1从Spm产生Spd，从norspermine产生norspermidine，证明其底物氧化模式类似于动物PAOs。据我们所知，AtPAO1是首个报道参与多胺回转途径的植物PAO。

• Purification and characterization of propylamine transferase from Sulfolobus solfataricus, an extreme thermophilic archaebacterium
  作者：Giovanna CACCIAPUOTI、Marina PORCELLI、Maria CARTENI-FARINA、Agata GAMBACORTA、Vincenzo ZAPPIA

  DOI：10.1111/j.1432-1033.1986.tb10442.x

  日期：1986.12

  The enzyme propylamine transferase, catalyzing the transfer of the propylamine moiety from S-adenosyl(5')-3-methylthiopropylamine to several amine acceptors, has been purified 643-fold in 20% yield from Sulfolobus solfataricus, an extreme thermophilic archaebacterium optimally growing at 87 degrees C. The purified enzyme (specific activity 2.05 units/mg protein), is homogeneous by criteria of gel electrophoresis, gel filtration, isoelectric focusing and ultracentrifugation analysis. The molecular mass of the native enzyme was estimated to be about 110 kDa by gel permeation and ultracentrifugation analysis. The protein migrates on SDS/polyacrylamide gel electrophoresis as a single band of 35 kDa, suggesting that the enzyme is a trimer composed by identical subunits. An optimum pH of 7.5 and an acidic isoelectric point of 5.3 have been calculated. The optimum temperature was 90 degrees C and no loss of activity is observable even after exposure of the purified enzyme to 100 degrees C for 1 h. No reducing agents are required for enzymatic activity. Substrate specificity towards the amine acceptors is rather broad in that 1,3-diaminopropane (Km = 1675 microM), putrescine (Km = 3850 microM), sym-norspermidine (Km = 954 microM) and spermidine (Km = 1539 microM) are recognized as substrates. Conversely S-adenosyl(5')-3-methylthiopropylamine is the only propylamine donor (Km = 7.9 microM) and the deamination of the sulfonium compound prevents the recognition by the enzyme. The reaction is irreversible and initial-rate kinetic studies indicate that the propylamine transfer is operated through a sequential mechanism. 5'-Methylthioadenosine, a product of the reaction, acts as a powerful competitive inhibitor with a Ki of 3.7 microM. Enzyme-substrate binding sites have been investigated with the aid of several substrate analogs and products. Among the compounds assayed, 5'-methylthiotubercidin, S-adenosyl(5')-3-thiopropylamine and S-adenosyl-3-thio-1,8-diaminooctane are the most active inhibitors.
• Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases from<i>Hyperthermus butylicus</i>and<i>Pyrobaculum aerophilum</i>
  作者：Jürgen Manfred Knott

  DOI：10.1016/j.febslet.2009.10.014

  日期：2009.11.3

  Polyamines are ubiquitously present in all organisms. In addition to the common polyamines, thermophilic archaea synthesize long‐chain polyamines. In the present study polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum were cloned and their substrate specificity was analyzed. The polyamine synthase HbSpeE II from H. butylicus synthesized long‐chain polyamines with high activity using the same mechanism that is used by a wide range of organisms to synthesize common polyamines, in which the aminopropyl residue derives from decarboxylated S‐adenosylmethionine. This is the first polyamine synthase described that synthesizes a polyamine longer than a tetramine with high activity.