(trimethylammonio)propionic acid iodide | 2812-22-8

• 分子结构分类: 有机化合物 - 有机氮化合物
• 英文名称: (trimethylammonio)propionic acid iodide
• 英文别名: (2-carboxy-ethyl)-trimethyl-ammonium; iodide；(2-Carboxy-aethyl)-trimethyl-ammonium; Jodid；2-Carboxy-N,N,N-trimethylethan-1-aminium iodide；2-carboxyethyl(trimethyl)azanium;iodide
• CAS: 2812-22-8
• 化学式: C₆H₁₄NO₂*I
• 分子量: 259.087
• InChiKey: LCFBLSBPJIUKLA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.83
• 重原子数：
  10
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  37.3
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (trimethylammonio)propionic acid iodide 在 anion exchange resin (OH^- form) 作用下， 以 水 为溶剂， 生成 三甲氨基丙酸内盐
  参考文献：
  名称：

  柔性两性离子分子在溶液中的电荷距离

  摘要：

  DOI：

  10.1021/j100368a013
• 作为产物：
  描述：

  Trimethyl(3-oxopropyl)azanium;iodide 在 Pisum sativum aminoaldehyde dehydrogenase 1 、 nicotinamide adenine dinucleotide 作用下， 生成 (trimethylammonio)propionic acid iodide
  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

文献信息

• Willstaetter, Chemische Berichte, 1902, vol. 35, p. 602
  作者：Willstaetter

  DOI：——

  日期：——
• Moser; Gubitz; Galvan, Arzneimittel-Forschung/Drug Research, 1995, vol. 45, # 4, p. 449 - 455
  作者：Moser、Gubitz、Galvan、Immel-Sehr、Lambrecht、Mutschler

  DOI：——

  日期：——
• Weiss, Archiv der Pharmazie, 1890, vol. 228, p. 187
  作者：Weiss

  DOI：——

  日期：——
• Structural and Functional Characterization of Plant Aminoaldehyde Dehydrogenase from Pisum sativum with a Broad Specificity for Natural and Synthetic Aminoaldehydes
  作者：Martina Tylichová、David Kopečný、Solange Moréra、Pierre Briozzo、René Lenobel、Jacques Snégaroff、Marek Šebela

  DOI：10.1016/j.jmb.2009.12.015

  日期：2010.3

  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.
• Intercharge distance of flexible zwitterionic molecules in solution
  作者：Yves. Chevalier、Pierre. Le Perchec

  DOI：10.1021/j100368a013

  日期：1990.3