(R)-2-amino-1-hydroxyethylphosphonic acid | 115511-00-7

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机膦酸及其衍生物
• 英文名称: (R)-2-amino-1-hydroxyethylphosphonic acid
• 英文别名: (1R)-(2-amino-1-hydroxyethyl)phosphonate；[(1R)-2-azaniumyl-1-hydroxyethyl]-hydroxyphosphinate
• CAS: 115511-00-7
• 化学式: C₂H₈NO₄P
• 分子量: 141.064
• InChiKey: RTTXIBKRJFIBBG-UWTATZPHSA-N

物化性质

• 沸点：
  497.5±55.0 °C(Predicted)
• 密度：
  1.714±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -5.3
• 重原子数：
  8
• 可旋转键数：
  2
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  104
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  (R)-2-amino-1-hydroxyethylphosphonic acid 生成 <2-(Benzoylamino)-1-(benzoyloxy)ethyl>phosphonsaeure-dimethylester
  参考文献：
  名称：

  Hammerschmidt, Friedrich, Liebigs Annalen der Chemie, 1988, p. 955 - 960

  摘要：

  DOI：
• 作为产物：
  描述：

  2-氨基乙基膦酸 在 PhnY α-ketoglutarate/Fe(II)-dependent dioxygenase 、 氧气 作用下， 生成 (R)-2-amino-1-hydroxyethylphosphonic acid
  参考文献：
  名称：

  PhnZ 与底物复合的晶体结构揭示了有机膦酸盐分解代谢的二铁加氧酶机制。

  摘要：

  PhnY 和 PhnZ 酶包含氧化分解代谢途径，使海洋细菌能够使用 2-氨基乙基膦酸作为无机磷酸盐的来源。PhnZ 以使用 Fe(II) 和双氧催化碳-磷键的氧化裂解而著称，尽管它属于水解酶的一个大家族，即 HD-磷酸水解酶超家族。我们已经确定了与其底物 (R)-2-amino-1-hydroxyethylphosphonate (2.1 A) 和缓冲添加剂 l-酒石酸盐 (1.7 A) 结合的 PhnZ 的高分辨率结构。这些结构表明 PhnZ 具有一个活性位点，其中包含由四个组氨酸和两个天冬氨酸配位的两个 Fe 离子，与碳-碳键裂解酶肌肉肌醇加氧酶极为相似。Y24 是个例外，它在 Fe2 的双氧结合位点形成瞬时配体相互作用。用底物类似物进行定点诱变和动力学分析揭示了关键活性位点残基的作用。第五个组氨酸在 PhnZ 亚分支中保守，H62，专门与底物 1-羟基相互作用。这些结构还表明，Y24

  DOI：

  10.1073/pnas.1320039111

文献信息

• An enantioselective synthesis of (R)-2-amino-1-hydroxyethylphosphonic acid by hydrolytic kinetic resolution of (±)-diethyl oxiranephosphonate
  作者：Peter B. Wyatt、Peter Blakskjær

  DOI：10.1016/s0040-4039(99)01259-9

  日期：1999.8

  (+/-)-Diethyl oxiranephosphonate undergoes efficient hydrolytic kinetic resolution by (R,R)-N,N'-bis(3,5-di-tert-butylsalicylidene)-1,2-cyclohexanediaminocobalt(III) acetate; opening of the resultant (R)-epoxide by benzylamine, followed by phosphonate ester hydrolysis and hydrogenolysis, affords the protozoal plasma membrane component (R)-2-amino-1-hydroxyethylphosphonic acid. (C) 1999 Elsevier Science Ltd. All rights reserved.

  (±)-二乙基氧化磷酯在(R,R)-N,N'-双(3,5-二叔丁基水杨酸)环己二胺钴(III)醋酸盐催化下，发生高效的水解动力学拆分，生成(R)-环氧化物。随后，苯胺开环(R)-环氧化物，经过磷酸酯的水解和氢解反应，最终得到原生动物的细胞膜成分(R)-2-氨基-1-羟基乙基磷酸。© 1999 Elsevier Science Ltd. 保留所有权利。
• Determination of the Absolute Configuration of (−)-Hydroxynitrilaphos and Related Biosynthetic Questions
  作者：Katharina Pallitsch、Barbara Happl、Christian Stieger

  DOI：10.1002/chem.201702904

  日期：2017.11.7

  On the mark: The absolute configuration of (−)-hydroxynitrilaphos from Streptomyces regensis WC-3744 was determined and a labeling strategy was developed to investigate the biosynthetic connection between hydroxynitrilaphos and hydroxyphosphonocystoximate.

  标记上：确定了来自瑞氏链霉菌WC-3744的（-）-羟基硝酰草胺的绝对构型，并制定了标记策略以研究羟基硝酰草胺与羟基膦酰基囊氧肟酸酯之间的生物合成联系。
• PhnY and PhnZ Comprise a New Oxidative Pathway for Enzymatic Cleavage of a Carbon–Phosphorus Bond
  作者：Fern R. McSorley、Peter B. Wyatt、Asuncion Martinez、Edward F. DeLong、Bjarne Hove-Jensen、David L. Zechel

  DOI：10.1021/ja302072f

  日期：2012.5.23

  family, cleave the carbon-phosphorus bond of the organophosphonate natural product 2-aminoethylphosphonic acid. PhnY adds a hydroxyl group to the α-carbon, yielding 2-amino-1-hydroxyethylphosphonic acid, which is oxidatively converted by PhnZ to inorganic phosphate and glycine. The PhnZ reaction represents a new enzyme mechanism for metabolic cleavage of a carbon-phosphorus bond.

  PhnY（一种α-酮戊二酸/Fe（II）依赖性双加氧酶）和 PhnZ（一种组氨酸天冬氨酸基序水解酶家族的 Fe（II）依赖性酶）的连续活性裂解有机膦酸盐天然产物的碳-磷键2-氨基乙基膦酸。PhnY 在 α-碳上添加一个羟基，产生 2-氨基-1-羟乙基膦酸，PhnZ 将其氧化转化为无机磷酸盐和甘氨酸。PhnZ 反应代表了一种新的酶机制，用于代谢裂解碳-磷键。
• Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases
  作者：Bigna Wörsdörfer、Mahesh Lingaraju、Neela H. Yennawar、Amie K. Boal、Carsten Krebs、J. Martin Bollinger、Maria-Eirini Pandelia

  DOI：10.1073/pnas.1315927110

  日期：2013.11.19

  Evolution functionally diversifies conserved protein architectures, precluding assignment of function from structure alone. The HD structural domain was first recognized in a group of phosphohydrolases and came to be associated with that activity, but characterization of the archetypal mixed-valent diiron oxygenase (MVDO), myo -inositol oxygenase, attributed a very different activity, O ₂ -mediated C-C bond cleavage, to an HD protein. We demonstrate that the recently discovered C-P bond-cleaving enzyme, PhnZ, is another example of an HD-domain MVDO. Sequence and functional data for the dimetal HD proteins reveal that they segregate into well-defined clades, of which several are more likely to comprise MVDOs than phosphohydrolases. This study provides a basis to assign hydrolase or oxygenase activity to proteins in this largely uncharacterized enzyme superfamily.

  进化通过功能多样化保守的蛋白质结构，防止仅从结构上赋予功能。HD结构域最初在一组磷酸水解酶中被认识，并与该活性相关，但是对原型混合价双铁氧化酶（MVDO）——myo-肌醇氧化酶的表征赋予了非常不同的活性，即O₂介导的C-C键断裂，属于HD蛋白质。我们证明，最近发现的C-P键断裂酶PhnZ是HD域MVDO的另一个例子。二金属HD蛋白质的序列和功能数据表明，它们分为明确定义的类群，其中几个类群更可能包含MVDO而不是磷酸水解酶。该研究为在这个大部分未被表征的酶超家族中赋予水解酶或氧化酶活性提供了基础。

• Enzymes in organic chemistry. Part 10: Chemo-enzymatic synthesis of l-phosphaserine and l-phosphaisoserine and enantioseparation of amino-hydroxyethylphosphonic acids by non-aqueous capillary electrophoresis with quinine carbamate as chiral ion pair agent
  作者：Friedrich Hammerschmidt、Wolfgang Lindner、Frank Wuggenig、Elfriede Zarbl

  DOI：10.1016/s0957-4166(00)00261-5

  日期：2000.7

  Diisopropyl 2-azido-1-acetoxyethylphosphonate (+/-)-7 was hydrolysed with high enantioselectivity by lipase SP 524 to give alpha-hydroxyphosphonate (S)-(-)-6 and ester (R)-(-)-7, which was saponified to give (R)-(+)-6. The two alpha-hydroxyphosphonates (R)- and (S)-6 were transformed into 1-phosphaisoserine and L-phosphaserine, respectively. Their enantiomeric excesses were determined to be 97% by HPLC on an chiral stationary phase. A mixture of all four stereoisomeric amino-hydroxyethylphosphonic acids can be separated by non-aqueous capillary electrophoresis with quinine carbamate as the chiral ion pair agent applying the partial filling technique. (C) 2000 Elsevier Science Ltd. All rights reserved.