dimethyl (L-1-amino)ethylphosphonate | 145240-97-7

• 分子结构分类: 有机化合物 - 有机酸及其衍生物
• 英文名称: dimethyl (L-1-amino)ethylphosphonate
• 英文别名: (R)-1-aminoethylphosphonic acid dimethyl ester；H-AlaP(OCH3)-OCH3；(1R)-1-dimethoxyphosphorylethanamine
• CAS: 145240-97-7
• 化学式: C₄H₁₂NO₃P
• 分子量: 153.118
• InChiKey: VVTZGGXICVHSRN-SCSAIBSYSA-N

物化性质

• 沸点：
  201.5±23.0 °C(Predicted)
• 密度：
  1.130±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.9
• 重原子数：
  9
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  61.6
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  氯甲酸苄酯 、 dimethyl (L-1-amino)ethylphosphonate 以 乙酸乙酯 为溶剂， 生成 dimethyl (L-1-benzoyloxycarbonylamino)ethylphosphonate
  参考文献：
  名称：

  An easy entry to optically active α-amino phosphonic acid derivatives using phase-transfer catalysis (PTC)

  摘要：

  在不对称亲水磷腈反应中空前绝后地使用相转移催化（PTC），使得直接从α-酰胺砜获得一系列光学活性的α-氨基膦酸衍生物成为可能。

  DOI：

  10.1039/b807027j
• 作为产物：
  描述：

  dimethyl (L-1-benzoyloxycarbonylamino)ethylphosphonate 在 氢气 作用下， 生成 dimethyl (L-1-amino)ethylphosphonate
  参考文献：
  名称：

  Synthesis ofN-acetylmuramic acid derivatives as potential inhibitors of the D-glutamic acid-adding enzyme

  摘要：

  Compounds containing N-acetyl-D-muramic acid and (L-1-aminoethyl)phosphonic acid were designed as potential inhibitors of the D-glutamic acid-adding enzyme of the biosynthesis of bacterial peptidoglycan. 2-Acetamido-2-deoxy-3-O-[(R)-2-propionyl-(L-1-aminoethyl)phosphonic acid]-D-glucopyranose (3) was synthesized. 2-Acetamido-1,4,6-tri-O-acetyl-2-deoxy-3-O-[(R)-2-propionyl- (L-l-aminoethyl) phosphonic acid dimethyl ester]-alpha,beta-D-glucopyranose (9) was also prepared and was submitted to the MacDonald reaction in order to introduce a phosphate group on the anomeric position. A complex mixture of phosphorylated or/and methylated derivatives of 3 was obtained. They were purified by h.p.l.c. and characterized by analyses of hexosamine, amino acid and labile phosphate, and by plasma desorption mass spectrometry. Neither 3 nor its derivatives inhibited the D-glutamic acid-adding enzyme from Escherichia coli.

  DOI：

  10.1002/prac.19953370176

文献信息

• (9H-Fluoren-9-yl)methanesulfonyl (Fms): An Amino Protecting Group Complementary to Fmoc
  作者：Yoshitaka Ishibashi、Kengo Miyata、Masato Kitamura

  DOI：10.1002/ejoc.201000682

  日期：2010.8

  developed. The advantages of this new PG were demonstrated in the successful formation of a phosphonamide between an N-Fms-protected α-phosphonoalanine monoester and secondary alkylamines, including (R)-2-phenylethylamine, (S)-phenylalanine tert-butyl ester (H-Phe-OtBu), H-Pro-Gly-OtBu, and H-Phe-Phe-OtBu, without formation of oxazaphospholine, which is a serious problem associated with the Fmoc PG

  开发了基于磺酰胺的保护基团 (PG)，(9H-芴-9-基) 甲磺酰基 (Fms)，其使用方式与成熟的 Fmoc PG 类似。这种新型 PG 的优势在 N-Fms 保护的 α-膦酰基丙氨酸单酯和仲烷基胺（包括 (R)-2-苯乙胺、(S)-苯丙氨酸叔丁酯 (H) -Phe-OtBu)、H-Pro-Gly-OtBu 和 H-Phe-Phe-OtBu，不会形成氧氮杂膦，这是与 Fmoc PG 相关的严重问题。这一成功应该为在基本上任意位置用 α-氨基膦酸 (AP) 取代的非天然肽的固相合成铺平道路，而无需对自 Carpino 在 1970 年的报告以来积累的基于 Fmoc 的化学进行重大修改。
• Penicillin G acylase-mediated kinetic resolution of racemic 1-( N -acylamino)alkylphosphonic and 1-( N -acylamino)alkylphosphinic acids and their esters
  作者：Katarzyna Zielińska、Roman Mazurkiewicz、Katarzyna Szymańska、Andrzej Jarzębski、Sylwia Magiera、Karol Erfurt

  DOI：10.1016/j.molcatb.2016.05.011

  日期：2016.10

  Extensive studies on the penicillin G acylase-mediated kinetic resolution of N-acylated 1-aminoalkylphosphonic and 1-aminoalkylphosphinic acids as well as their esters were carried out to recognise the relationships between the substrate structure, reaction conditions, and the enzymatic hydrolytic deacylation efficiency and stereoselectivity. Reactivity of 1-(N-acylamino)alkylphosphonic and 1-(N-acylamino)allcylphosphinic acids and their esters in the penicillin G acylase-mediated hydrolytic deacylation reaction depends strongly on the kind of their N-acyl group, with high preference to the hydrolytic splitting of the N-phenylacetyl moiety. The initial hydrolysis rates of 1-(N-phenylacetylamino)alkylphosphonic acid dimethyl esters 2 are mostly distinctly lower in comparison with the corresponding free acids 3 and rapidly decrease with the increasing steric effect of the substituent at the alpha-position. In contrary to the substituents at the alpha-carbon, bulky substituents at the phosphorus hinder the enzymatic hydrolysis to a much lesser degree. The penicillin G acylase-mediated stereospecific hydrolysis of N-acyl group of both racemic 1-(N-acylamino)alkylphosphonic acids 3 and their dimethyl esters 2 proved to be, in most cases, a highly effective method for the kinetic resolution of these compounds: High enzyme enantioselectivity E-values exceeding 100, or synthetically useful E-values exceeding 20 (in two cases) were obtained for the N-acylated phosphonic acid analogues of alanine, phenylalanine, valine, leucine, and asparagine, as well as for their dimethyl esters, with the exception of the dimethyl ester of phosphonic analogue of valine 2e, that E-value was low (E=1.2). Also for the N-acylated H-phosphinic acid analogues of alanine, as well as phenylphosphinic acid analogue of alanine, high enzyme enantioselectivity values exceeding 100 were obtained. In contrary, E-values for both diastereomers of ethyl ester of phenylphosphinic analogue of alanine 2k were low (E=7 and 13). For the all accomplished assignments penicillin G acylase exhibited stereochemical preference for the (R)-substrate. (C) 2016 Elsevier B.V. All rights reserved.
• Batch and in-flow kinetic resolution of racemic 1-(N-acylamino)alkylphosphonic and 1-(N-acylamino)alkylphosphinic acids and their esters using immobilized penicillin G acylase
  作者：Katarzyna Zielińska、Katarzyna Szymańska、Roman Mazurkiewicz、Andrzej Jarzębski

  DOI：10.1016/j.tetasy.2016.11.007

  日期：2017.1

  The kinetic resolution of racemic 1-(N-acylamino)alkylphosphonic acids 3 (R-3 = OH) and their dimethyl esters 1, as well as 1-(N-acylamino)alkylphosphinic acids 4 (R-3 = H or Ph) using penicillin G acylase (PGA) immobilized on three types of mesoporous silicas in both a batch slurry system and in a continuous-flow reactor was studied. The initial hydrolytic deacylation rates in the presence of those catalysts were measured and the relationships between the substrate structure and the enzyme efficiency are discussed. The stereospecific hydrolysis of the N-acyl group of both racemic N-acylated phosphorus analogues of amino acids and their esters catalyzed by the immobilized PGA proved to be a highly effective method for the kinetic resolution of all the investigated compounds, with the stereochemical preference of PGA for (R)-substrates. (C) 2016 Elsevier Ltd. All rights reserved.