2-amino-ethanol; protonated form | 22852-66-0

• 分子结构分类: 有机化合物 - 有机氮化合物
• 英文名称: 2-amino-ethanol; protonated form
• 英文别名: (2-hydroxyethyl)-ammonium cation；2-Aminoethanol;hydron
• CAS: 22852-66-0
• 化学式: C₂H₈NO
• 分子量: 62.0916
• InChiKey: HZAXFHJVJLSVMW-UHFFFAOYSA-O

计算性质

• 辛醇/水分配系数(LogP)：
  -1.3
• 重原子数：
  4
• 可旋转键数：
  1
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  47.9
• 氢给体数：
  2
• 氢受体数：
  1

反应信息

• 作为反应物：
  描述：

  2-amino-ethanol; protonated form 生成 乙醛 、 铵
  参考文献：
  名称：

  钴胺素依赖性脱水酶和脱氨酶：自由基催化和重新活化伴侣。

  摘要：

  腺苷钴胺素是维生素B12的一种辅酶形式，是一种有机金属化合物，参与约十种酶促反应。这些酶通过使用源自辅酶Co-C键均质化的高反应性伯碳自由基来催化化学挑战性反应。其中，对二醇脱水酶和乙醇胺氨裂解酶进行了最广泛的研究，以建立腺苷钴胺素辅助酶催化和自由基催化反应的一般机理。另一个重要的点是，腺苷钴胺素依赖性自由基酶在催化过程中易于发生基于机理的不可逆失活，并且具有自己的伴侣分子来维持催化活性。这篇评论将重点介绍生物化学，结构，

  DOI：

  10.1016/j.abb.2013.11.002
• 作为产物：
  描述：

  C.I.酸性橙108 在 dimethylammonium 作用下， 生成 2-amino-ethanol; protonated form
  参考文献：
  名称：

  Internal and external solvation of polyfunctional ions

  摘要：

  DOI：

  10.1021/ja00541a001

文献信息

• Differential Role of Human Choline Kinase α and β Enzymes in Lipid Metabolism: Implications in Cancer Onset and Treatment
  作者：David Gallego-Ortega、Ana Ramirez de Molina、Maria Angeles Ramos、Fatima Valdes-Mora、Maria Gonzalez Barderas、Jacinto Sarmentero-Estrada、Juan Carlos Lacal

  DOI：10.1371/journal.pone.0007819

  日期：——

  Background The Kennedy pathway generates phosphocoline and phosphoethanolamine through its two branches. Choline Kinase (ChoK) is the first enzyme of the Kennedy branch of synthesis of phosphocholine, the major component of the plasma membrane. ChoK family of proteins is composed by ChoKα and ChoKβ isoforms, the first one with two different variants of splicing. Recently ChoKα has been implicated in the carcinogenic process, since it is over-expressed in a variety of human cancers. However, no evidence for a role of ChoKβ in carcinogenesis has been reported. Methodology/Principal Findings Here we compare the in vitro and in vivo properties of ChoKα1 and ChoKβ in lipid metabolism, and their potential role in carcinogenesis. Both ChoKα1 and ChoKβ showed choline and ethanolamine kinase activities when assayed in cell extracts, though with different affinity for their substrates. However, they behave differentially when overexpressed in whole cells. Whereas ChoKβ display an ethanolamine kinase role, ChoKα1 present a dual choline/ethanolamine kinase role, suggesting the involvement of each ChoK isoform in distinct biochemical pathways under in vivo conditions. In addition, while overexpression of ChoKα1 is oncogenic when overexpressed in HEK293T or MDCK cells, ChoKβ overexpression is not sufficient to induce in vitro cell transformation nor in vivo tumor growth. Furthermore, a significant upregulation of ChoKα1 mRNA levels in a panel of breast and lung cancer cell lines was found, but no changes in ChoKβ mRNA levels were observed. Finally, MN58b, a previously described potent inhibitor of ChoK with in vivo antitumoral activity, shows more than 20-fold higher efficiency towards ChoKα1 than ChoKβ. Conclusion/Significance This study represents the first evidence of the distinct metabolic role of ChoKα and ChoKβ isoforms, suggesting different physiological roles and implications in human carcinogenesis. These findings constitute a step forward in the design of an antitumoral strategy based on ChoK inhibition.

  背景 肯尼迪途径通过其两个分支产生磷脂酰胆碱和磷脂酰乙醇胺。胆碱激酶（ChoK）是肯尼迪途径合成磷脂酰胆碱的第一种酶，磷脂酰胆碱是血浆膜的主要成分。胆碱激酶家族由ChoKα和ChoKβ同工型组成，前者有2种不同的剪接变体。最近，ChoKα被证实与致癌过程有关，因为它会在多种人类癌症中过度表达。然而，目前尚无证据表明ChoKβ在致癌过程中发挥作用。 方法/主要发现 在此，我们比较了ChoKα1和ChoKβ在脂质代谢中的体外和体内特性，以及它们在致癌过程中的潜在作用。在细胞提取物中检测时，ChoKα1和ChoKβ均表现出胆碱和乙醇胺激酶活性，尽管它们对底物的亲和力不同。然而，当它们在整细胞中过度表达时，它们的行为会有所不同。ChoKβ表现出乙醇胺激酶的作用，而ChoKα1则表现出胆碱/乙醇胺双激酶的作用，这表明在体内条件下，每种ChoK同工型都参与不同的生化途径。此外，当在HEK293T或MDCK细胞中过度表达ChoKα1时，它会产生致癌作用，而ChoKβ的过度表达则不足以诱导体外细胞转化或体内肿瘤生长
• Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily
  作者：A. J. Stewart、R. Schmid、C. A. Blindauer、S. J. Paisey、C. Farquharson

  DOI：10.1093/protein/gzg126

  日期：2003.12.1

  PHOSPHO1 is a recently identified phosphatase whose expression is upregulated in mineralizing cells and is implicated in the generation of inorganic phosphate for matrix mineralization, a process central to skeletal development. The enzyme is a member of the haloacid dehalogenase (HAD) superfamily of magnesium‐dependent hydrolases. However, the natural substrate(s) is as yet unidentified and to date no structural information is known. We have identified homologous proteins in a number of species and have modelled human PHOSPHO1 based upon the crystal structure of phosphoserine phosphatase (PSP) from Methanococcus jannaschii. The model includes the catalytic Mg2+ atom bound via three conserved Asp residues (Asp32, Asp34 and Asp203); O‐ligands are also provided by a phosphate anion and two water molecules. Additional residues involved in PSP‐catalysed hydrolysis are conserved and are located nearby, suggesting both enzymes share a similar reaction mechanism. In PHOSPHO1, none of the PSP residues that confer the enzyme’s substrate specificity (Arg56, Glu20, Met43 and Phe49) are conserved. Instead, we propose that two fully conserved Asp residues (Asp43 and Asp123), not present in PSPs contribute to substrate specificity in PHOSPHO1. Our findings show that PHOSPHO1 is not a member of the subfamily of PSPs but belongs to a novel, closely related enzyme group within the HAD superfamily.

  PHOSPHO1 是最近发现的一种磷酸酶，其表达在矿化细胞中上调，与基质矿化过程中无机磷酸盐的生成有关，这是骨骼发育的一个核心过程。该酶是依赖镁的水解酶卤酸脱卤酶（HAD）超家族的成员。然而，该酶的天然底物尚未确定，结构信息也尚不清楚。我们已经确定了一些物种中的同源蛋白，并根据梅氏球菌（Methanococcus jannaschii）磷酸丝氨酸磷酸酶（PSP）的晶体结构建立了人类 PHOSPHO1 的模型。该模型包括通过三个保守的 ASP 残基（ASP32、ASP34 和 ASP203）结合的催化 Mg2+ 原子；磷酸阴离子和两个水分子也提供了 O 配体。参与 PSP 催化水解的其他残基也是保守的，而且位于附近，这表明这两种酶具有相似的反应机制。在 PHOSPHO1 中，赋予该酶底物特异性的 PSP 残基（Arg56、Glu20、Met43 和 Phe49）都没有保守。相反，我们认为两个完全保守的 ASP 残基（ASP43 和 ASP123）不存在于 PSP 中，它们有助于 PHOSPHO1 的底物特异性。我们的研究结果表明，PHOSPHO1 不是 PSPs 亚家族的成员，而是属于 HAD 超家族中一个新的、密切相关的酶组。
• Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities
  作者：Scott J. ROBERTS、Alan J. STEWART、Peter J. SADLER、Colin FARQUHARSON

  DOI：10.1042/bj20040511

  日期：2004.8.15

  Human PHOSPHO1 is a phosphatase enzyme for which expression is upregulated in mineralizing cells. This enzyme has been implicated in the generation of Pi for matrix mineralization, a process central to skeletal development. PHOSPHO1 is a member of the haloacid dehalogenase (HAD) superfamily of Mg2+-dependent hydrolases. However, substrates for PHOSPHO1 are, as yet, unidentified and little is known about its activity. We show here that PHOSPHO1 exhibits high specific activities toward phosphoethanolamine (PEA) and phosphocholine (PCho). Optimal enzymic activity was observed at approx. pH 6.7. The enzyme shows a high specific Mg2+-dependence, with apparent Km values of 3.0 μM for PEA and 11.4 μM for PCho. These results provide a novel mechanism for the generation of Pi in mineralizing cells from PEA and PCho.

  人类 PHOSPHO1 是一种在矿化细胞中表达上调的磷酸酶。这种酶与基质矿化所需的π的生成有关，而基质矿化是骨骼发育的核心过程。PHOSPHO1 是 Mg2+ 依赖性水解酶卤酸脱卤酶（HAD）超家族的成员。然而，PHOSPHO1 的底物尚未确定，对其活性也知之甚少。我们在这里发现，PHOSPHO1 对磷酸乙醇胺（PEA）和磷酸胆碱（PCho）具有很高的特异性活性。在 pH 值约为 6.7 时观察到了最佳的酶活性。该酶显示出高度的特异性 Mg2+ 依赖性，对 PEA 的表观 Km 值为 3.0 μM，对 PCho 的表观 Km 值为 11.4 μM。这些结果为矿化细胞中 PEA 和 PCho 产生 Pi 提供了一种新的机制。
• Phosphorylcholine Phosphatase: A Peculiar Enzyme of <i>Pseudomonas aeruginosa</i>
  作者：Carlos Eduardo Domenech、Lisandro Horacio Otero、Paola Rita Beassoni、Angela Teresita Lisa

  DOI：10.4061/2011/561841

  日期：2011.9.11

  Pseudomonas aeruginosa synthesizes phosphorylcholine phosphatase (PchP) when grown on choline, betaine, dimethylglycine or carnitine. In the presence of Mg²⁺ or Zn²⁺, PchP catalyzes the hydrolysis of p-nitrophenylphosphate (p-NPP) or phosphorylcholine (Pcho). The regulation of pchP gene expression is under the control of GbdR and NtrC; dimethylglycine is likely the metabolite directly involved in the induction of PchP. Therefore, the regulation of choline metabolism and consequently PchP synthesis may reflect an adaptive response of P. aeruginosa to environmental conditions. Bioinformatic and biochemistry studies shown that PchP contains two sites for alkylammonium compounds (AACs): one in the catalytic site near the metal ion-phosphoester pocket, and another in an inhibitory site responsible for the binding of the alkylammonium moiety. Both sites could be close to each other and interact through the residues ⁴²E, ⁴³E and ⁸²YYY⁸⁴. Zn²⁺ is better activator than Mg²⁺ at pH 5.0 and it is more effective at alleviating the inhibition produced by the entry of Pcho or different AACs in the inhibitory site. We postulate that Zn²⁺ induces at pH 5.0 a conformational change in the active center that is communicated to the inhibitory site, producing a compact or closed structure. However, at pH 7.4, this effect is not observed because to the hydrolysis of the [Zn²⁺L₂⁻¹L₂⁰(H₂O)₂] complex, which causes a change from octahedral to tetrahedral in the metal coordination geometry. This enzyme is also present in P. fluorescens, P. putida, P. syringae, and other organisms. We have recently crystallized PchP and solved its structure.

  当以胆碱、甜菜碱、二甲基甘氨酸或肉碱为基质时，铜绿假单胞菌（Pseudomonas aeruginosa）会合成磷酸胆碱酯酶（PchP）。在Mg2+或Zn2+存在下，PchP可催化对硝基苯磷酸酯（p-NPP）或磷酸胆碱（Pcho）的水解。PchP基因表达的调控受GbdR和NtrC的控制；二甲基甘氨酸很可能是直接参与诱导PchP的代谢产物。因此，胆碱代谢及PchP合成的调控可能反映了铜绿假单胞菌对环境条件的适应性反应。生物信息学和生物化学研究表明，PchP含有两个烷基铵化合物（AACs）位点：一个位于金属离子-磷酸酯口袋附近的催化位点，另一个是抑制位点，负责结合烷基铵基团。这两个位点可能彼此靠近并通过残基42E、43E和82YYY84相互作用。在pH 5.0下，Zn2+是比Mg2+更好的激活剂，并且在缓解Pcho或不同AACs进入抑制位点产生的抑制作用方面更有效。我们假设Zn2+在pH 5.0下诱导了活性中心的构象变化，并传递到抑制位点，产生了一种紧凑或封闭的结构。然而，在pH 7.4下，由于[Zn2+L2-1L20(H2O)2]配合物的水解，从八面体到四面体的金属配位几何结构的改变，这种效应没有观察到。这种酶也存在于铜绿假单胞菌的其他菌株中，如荧光铜绿假单胞菌（P. fluorescens）、铜绿假单胞菌（P. putida）和疫病铜绿假单胞菌（P. syringae）。我们最近结晶了PchP并解析了其结构。
• <i>Escherichia coli</i> Cytosolic Glycerophosphodiester Phosphodiesterase (UgpQ) Requires Mg ²⁺ , Co ²⁺ , or Mn ²⁺ for Its Enzyme Activity
  作者：Noriyasu Ohshima、Saori Yamashita、Naoko Takahashi、Chizu Kuroishi、Yoshitsugu Shiro、Koji Takio

  DOI：10.1128/jb.01223-07

  日期：2008.2.15

  Escherichia coli cytosolic glycerophosphodiester phosphodiesterase, UgpQ, functions in the absence of other proteins encoded by the ugp operon and requires Mg ²⁺ , Mn ²⁺ , or Co ²⁺ , in contrast to Ca ²⁺ -dependent periplasmic glycerophosphodiester phosphodiesterase, GlpQ. UgpQ has broad substrate specificity toward various glycerophosphodiesters, producing sn -glycerol-3-phosphate and the corresponding alcohols. UgpQ accumulates under conditions of phosphate starvation, suggesting that it allows the utilization of glycerophosphodiesters as a source of phosphate. These results clarify how E. coli utilizes glycerophosphodiesters using two homologous enzymes, UgpQ and GlpQ.

  摘要 大肠杆菌 细胞膜甘油磷酸二酯磷酸二酯酶 UgpQ 在没有其他由 ugp 操作子编码的其他蛋白的情况下发挥作用，并且需要 Mg 2+ 、Mn 2+ 或 Co 2+ 与 Ca 2+ -依赖的质膜周围甘油磷酸二酯磷酸二酯酶 GlpQ 相反。UgpQ 对各种甘油磷酸二酯具有广泛的底物特异性，可产生 sn -甘油-3-磷酸酯和相应的醇。UgpQ 在磷酸盐饥饿条件下会积累，这表明它可以利用甘油磷酸二酯作为磷酸盐的来源。这些结果澄清了 大肠杆菌 是如何利用两种同源酶 UgpQ 和 GlpQ 来利用甘油磷酸二酯的。