4-氨基丁醛 | 4390-05-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 中文名称: 4-氨基丁醛
• 中文别名: 1-氨基-9,10-二氢-4-羟基-9,10-二羰基蒽-2-磺基酸
• 英文名称: 4-aminobutyraldehyde
• 英文别名: 4-aminobutanal
• CAS: 4390-05-0
• 化学式: C₄H₉NO
• mdl: MFCD19203452
• 分子量: 87.1216
• InChiKey: DZQLQEYLEYWJIB-UHFFFAOYSA-N

物化性质

• 沸点：
  159.9±23.0 °C(Predicted)
• 密度：
  0.911±0.06 g/cm3(Predicted)
• 物理描述：
  Solid

计算性质

• 辛醇/水分配系数(LogP)：
  -0.9
• 重原子数：
  6
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  43.1
• 氢给体数：
  1
• 氢受体数：
  2

安全信息

• 海关编码：
  2922399090

反应信息

• 作为反应物：
  描述：

  4-氨基丁醛 在 Pisum sativum aminoaldehyde dehydrogenase 1 、 nicotinamide adenine dinucleotide 作用下， 生成 4-氨基丁酸
  参考文献：
  名称：

  Structural and Functional Characterization of Plant Aminoaldehyde Dehydrogenase from Pisum sativum with a Broad Specificity for Natural and Synthetic Aminoaldehydes

  摘要：

  Aminoaldehyde dehydrogenases (AMADHs, EC 1.2.1.19) belong to the large aldehyde dehydrogenase (ALDH) superfamily, namely, the ALDH9 family. They oxidize polyamine-derived omega-aminoaldehydes to the corresponding omega-amino acids. Here, we report the first X-ray structures of plant AMADHs: two isoenzymes, PsAMADH1 and PsAMADH2, from Pisum sativum in complex with beta-nicotinamide adenine dinucleotide (NAD(+)) at 2.4 and 2.15 angstrom resolution, respectively. Both recombinant, proteins are dimeric and, similarly to other ALDHs, each monomer is composed of an oligomerization domain, a coenzyme binding domain and a catalytic domain. Each subunit binds NAD(+) as a coenzyme, contains a solvent-accessible C-terminal peroxisomal targeting signal (type 1) and a cation bound in the cavity close to the NAD(+) binding site. While the NAD(+) binding mode is classical for PsAMADH2, that for PsAMADH1 is unusual among ALDHs. A glycerol molecule occupies the substrate binding site and mimics a bound substrate. Structural analysis and substrate specificity study of both isoenzymes in combination with data published previously on other ALDH9 family members show that the established categorization of such enzymes into distinct groups based on substrate specificity is no more appropriate, because many of them seem capable of oxidizing a large spectrum of aminoaldehyde substrates. PsAMADH1 and PsAMADH2 can oxidize N,N,N-trimethyl-4-aminobutyraldehyde into gamma-butyrobetaine, which is the carnitine precursor in animal cells. This activity highly suggests that in addition to their contribution to the formation of compatible osmolytes such as glycine betaine, beta-alanine betaine and gamma-aminobutyric acid, AMADHs might participate in carnitine biosynthesis in plants. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.jmb.2009.12.015
• 作为产物：
  描述：

  3,4-二氢-2H-吡咯 在 Dowex-50 (H⁺) 、 水 作用下， 生成 4-氨基丁醛
  参考文献：
  名称：

  玉米多胺氧化酶的表征

  摘要：

  已经检查了从玉米芽中纯化的多胺氧化酶 (PAO) 的一些结构和生化特征。该酶仅具有丙氨酸作为 N 端氨基酸，其 N 端序列与来自丁香假单胞菌的色氨酸 2-单加氧酶具有显着的同源性。萨瓦斯塔诺伊 天然酶稳定性的最适 pH 值为 5，类似于大麦叶酶的 pH 值。量热分析显示在 pH 6 时 Tm 为 49.8 度的单个双态转变。在 pH 值为 5 时，热稳定性提高了 14 度以上。胺氧化产物 delta 1-吡咯啉和 diazabicyclononane，是 PAO 活性的竞争性抑制剂（表观 Ki = 400 和 100 microM）。此外，这些化合物提高了酶的热稳定性。N1-乙酰精胺，

  DOI：

  10.1016/0031-9422(90)85157-b

文献信息

• Clean and Highly Selective Oxidation of Alcohols by the PhI(OAc)₂/Mn(TPP)CN/Im Catalytic System
  作者：Gholam Reza Karimipour、Hamid Asadpour Shadegan、Roxana Ahmadpour

  DOI：10.3184/030823407x209679

  日期：2007.4

  An efficient method for the oxidation of alcohols is presented. Using catalytic amounts of manganese porphyrin [Mn(TPP)CN] in combination with (diacetoxyiodo)benzene (PhI(OAc)2) allows the conversion of benzylic and primary aliphatic and aromatic alcohols into the corresponding aldehydes, and secondary alcohols to ketones as the sole products. This method provides a cost-effective and environmentally

  提出了一种有效的醇氧化方法。使用催化量的锰卟啉 [Mn(TPP)CN] 与（二乙酰氧基碘）苯（PhI(OAc)2）结合，可以将苄基和伯脂肪族和芳族醇转化为相应的醛，将仲醇转化为酮作为唯一的产品。由于使用了毒性较低的 PhI(OAc)2 和生物相关的锰卟啉，该方法提供了一种经济高效且环境友好的氧化过程。产物的量（%）和选择性很大程度上取决于金属卟啉催化剂的性质以及起始醇的电子和空间性质。
• Hydrophobicity dependence of oxidation of tetrapeptides of elastin sequences with Mn(III): Synthesis, characterization, kinetics, and mechanistic study
  作者：B. K. Kempe Gowda、H. S. Prasad、K. S. Rangappa、D. Channe Gowda

  DOI：10.1002/kin.10015

  日期：2002.1

  The analogues of elastin sequences, glycyl-glycyl-alanyl-proline (GGAP), glycyl-glycyl-phenylalanyl-proline (GGFP), and glycyl-glycyl-isoleucyl-proline (GGIP) were synthesized by classical solution phase method and characterized. The kinetics of oxidation of these tetrapeptides (TETP) by Mn(III) has been studied in the presence of sulphate ions in acidic solution at 25°C. The reaction was followed

  弹性蛋白序列的类似物，甘氨酰-甘氨酰-丙氨酰-脯氨酸(GGAP)、甘氨酰-甘氨酰-苯丙氨酰-脯氨酸(GGFP)和甘氨酰-甘氨酰-异亮氨酰-脯氨酸(GGIP)通过经典液相法合成并表征。在 25°C 酸性溶液中存在硫酸根离子的情况下，研究了 Mn(III) 对这些四肽 (TETP) 的氧化动力学。在 λmax = 500 nm 处用分光光度法跟踪反应。观察到速率对 [Mn(III)] 和 [TETP] 的一级依赖性。该速率与还原产物、Mn(II) 和氢离子的浓度无关。研究了改变介质介电常数和添加阴离子（如硫酸盐、氯化物或高氯酸盐）的影响。激活参数已使用 Arrhenius 和 Erying 图进行了评估。氧化产物被分离和表征。提出了在限速步骤中涉及 TETP 与 Mn(III) 反应的机制。在这些序列的氧化速率和疏水性之间注意到明显的相关性，其中增加的疏水性导致增加的氧化速率。© 2001 John
• Role and structural characterization of plant aldehyde dehydrogenases from family 2 and family 7
  作者：Radka Končitíková、Armelle Vigouroux、Martina Kopečná、Tomáš Andree、Jan Bartoš、Marek Šebela、Solange Moréra、David Kopečný

  DOI：10.1042/bj20150009

  日期：2015.5.15

  Aldehyde dehydrogenases (ALDHs) are responsible for oxidation of biogenic aldehyde intermediates as well as for cell detoxification of aldehydes generated during lipid peroxidation. So far, 13 ALDH families have been described in plants. In the present study, we provide a detailed biochemical characterization of plant ALDH2 and ALDH7 families by analysing maize and pea ALDH7 (ZmALDH7 and PsALDH7) and four maize cytosolic ALDH(cALDH)2 isoforms RF2C, RF2D, RF2E and RF2F [the first maize ALDH2 was discovered as a fertility restorer (RF2A)]. We report the crystal structures of ZmALDH7, RF2C and RF2F at high resolution. The ZmALDH7 structure shows that the three conserved residues Glu120, Arg300 and Thr302 in the ALDH7 family are located in the substrate-binding site and are specific to this family. Our kinetic analysis demonstrates that α-aminoadipic semialdehyde, a lysine catabolism intermediate, is the preferred substrate for plant ALDH7. In contrast, aromatic aldehydes including benzaldehyde, anisaldehyde, cinnamaldehyde, coniferaldehyde and sinapaldehyde are the best substrates for cALDH2. In line with these results, the crystal structures of RF2C and RF2F reveal that their substrate-binding sites are similar and are formed by an aromatic cluster mainly composed of phenylalanine residues and several nonpolar residues. Gene expression studies indicate that the RF2C gene, which is strongly expressed in all organs, appears essential, suggesting that the crucial role of the enzyme would certainly be linked to the cell wall formation using aldehydes from phenylpropanoid pathway as substrates. Finally, plant ALDH7 may significantly contribute to osmoprotection because it oxidizes several aminoaldehydes leading to products known as osmolytes.

  醛脱氢酶（ALDHs）负责生物醛中间产物的氧化以及脂质过氧化过程中产生的醛的细胞解毒。迄今为止，植物中已描述了 13 个 ALDH 家族。在本研究中，我们通过分析玉米和豌豆的 ALDH7（ZmALDH7 和 PsALDH7）以及四种玉米细胞质 ALDH（cALDH）2 异构体 RF2C、RF2D、RF2E 和 RF2F，对植物 ALDH2 和 ALDH7 家族进行了详细的生化鉴定[发现的第一个玉米 ALDH2 是一种生育力恢复剂（RF2A）]。我们报告了 ZmALDH7、RF2C 和 RF2F 的高分辨率晶体结构。ZmALDH7 的结构表明，ALDH7 家族中的三个保守残基 Glu120、Arg300 和 Thr302 位于底物结合位点，并且是该家族所特有的。我们的动力学分析表明，α-氨基己二酸半醛是赖氨酸分解代谢的中间产物，是植物 ALDH7 的首选底物。相比之下，芳香醛（包括苯甲醛、茴香醛、肉桂醛、针叶醛和山奈醛）是 cALDH2 的最佳底物。与这些结果相一致，RF2C 和 RF2F 的晶体结构显示，它们的底物结合位点相似，都是由一个主要由苯丙氨酸残基和几个非极性残基组成的芳香族簇构成。基因表达研究表明，RF2C 基因在所有器官中都有很强的表达，似乎是必不可少的，这表明该酶的关键作用肯定与以苯丙醛途径中的醛为底物形成细胞壁有关。最后，植物的 ALDH7 可能对渗透保护有重大贡献，因为它能氧化多种氨基醛，产生被称为渗透溶质的产物。
• An Engineered Alcohol Oxidase for the Oxidation of Primary Alcohols
  作者：Rachel S. Heath、William R. Birmingham、Matthew P. Thompson、Andreas Taglieber、Laurent Daviet、Nicholas J. Turner

  DOI：10.1002/cbic.201800556

  日期：——

  Turn up the heat: Alcohol oxidases require no cofactor or cofactor recycling system for catalysis, just O2, but their use is limited by activity and substrate scope. An alcohol oxidase with a broad scope for primary alcohol oxidations has now been evolved. Further improvements were made to enzyme stability and demonstrated by its increased thermostability and solvent tolerance.

  调高热量：醇氧化酶不需要催化的辅助因子或辅助因子循环系统，只需O 2即可，但其使用受到活性和底物范围的限制。现在已经开发出具有广泛伯醇氧化范围的醇氧化酶。酶的稳定性得到了进一步的改善，并通过增加的热稳定性和耐溶剂性得到证明。
• Amino Aldehydes Revisited
  作者：Luuk Mestrom、Paula Bracco、Ulf Hanefeld

  DOI：10.1002/ejoc.201701213

  日期：2017.12.22

  The enzymatic oxidation of amino alcohols was studied to address the long-standing problem of product stability. Amino aldehydes, the much sought after and unstable compounds, can be generated under mild conditions when they are immediately protected. Utilizing a range of alcohol dehydrogenases (ADHs) and semicarbazide as scavenger, the enantioselective synthesis of protected amino aldehydes is possible

  研究氨基醇的酶促氧化以解决长期存在的产品稳定性问题。氨基醛是备受追捧的不稳定化合物，当它们立即受到保护时，可以在温和条件下生成。利用一系列醇脱氢酶 (ADH) 和氨基脲作为清除剂，可以对受保护的氨基醛进行对映选择性合成。来自氧化葡糖杆菌 (GoGDH) 的甘油脱氢酶显示出优异的对映选择性，但底物范围有限，而马肝 ADH 催化广泛的转化，但对映选择性较低。