D-1-(N-phenylacetylamino)ethylphosphonic acid | 130325-37-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: D-1-(N-phenylacetylamino)ethylphosphonic acid
• 英文别名: (S)-1-(N-phenylacetylamino)ethylphosphonic acid；[(1S)-1-[(2-phenylacetyl)amino]ethyl]phosphonic acid
• CAS: 130325-37-0
• 化学式: C₁₀H₁₄NO₄P
• 分子量: 243.199
• InChiKey: VMDVDXQQISYHAV-QMMMGPOBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.2
• 重原子数：
  16
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  86.6
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  D-1-(N-phenylacetylamino)ethylphosphonic acid 反应 72.0h， 以75%的产率得到(S)-(+)-1-氨基乙基膦酸
  参考文献：
  名称：

  Enzymatic preparation of both L- and D-enantiomers of phosphonic and phosphonous analogues of alanine using penicillin acylase

  摘要：

  D-Enantiomers of N-acylated 1-aminoethylphosphonic and 1-aminoethylphosphonous acids were able to be hydrolyzed with high concentrations of penicillin acylase in a reasonable time period. This finding was used to prepare both L- and D-enantiomers of these phosphorus analogues of alanine by stepwise enzymatic hydrolysis of their racemic N-phenylacetyl derivatives using the same enzyme - penicillin acylase - by simply changing the enzyme/substrate ratio.

  DOI：

  10.1016/s0957-4166(00)82240-5
• 作为产物：
  描述：

  1-(N-phenylacetylamino)ethylphosphonic acid 生成 D-1-(N-phenylacetylamino)ethylphosphonic acid
  参考文献：
  名称：

  Enzymatic preparation of both L- and D-enantiomers of phosphonic and phosphonous analogues of alanine using penicillin acylase

  摘要：

  D-Enantiomers of N-acylated 1-aminoethylphosphonic and 1-aminoethylphosphonous acids were able to be hydrolyzed with high concentrations of penicillin acylase in a reasonable time period. This finding was used to prepare both L- and D-enantiomers of these phosphorus analogues of alanine by stepwise enzymatic hydrolysis of their racemic N-phenylacetyl derivatives using the same enzyme - penicillin acylase - by simply changing the enzyme/substrate ratio.

  DOI：

  10.1016/s0957-4166(00)82240-5

文献信息

• 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.
• SHVYADAS, V. -YU. K.;SOLODENKO, V. A.;KOZLOVA, E. V.;KASHEVA, T. N.;KUXAR+
  作者：SHVYADAS, V. -YU. K.、SOLODENKO, V. A.、KOZLOVA, E. V.、KASHEVA, T. N.、KUXAR+

  DOI：——

  日期：——
• Kukhar, Valery; Solodenko, Vladimir; Soloshonok, Vadim, Phosphorus, Sulfur and Silicon and the Related Elements, 1996, vol. 109, # 1-4, p. 529 - 532
  作者：Kukhar, Valery、Solodenko, Vladimir、Soloshonok, Vadim、Kasheva, Tamara

  DOI：——

  日期：——
• Enzymatic preparation of both L- and D-enantiomers of phosphonic and phosphonous analogues of alanine using penicillin acylase
  作者：Vladimir A. Solodenko、Michail Y. Belik、Sergei V. Galushko、Valeri P. Kukhar、Elena V. Kozlova、Dmitri A. Mironenko、Vitas K. Svedas

  DOI：10.1016/s0957-4166(00)82240-5

  日期：1993.1

  D-Enantiomers of N-acylated 1-aminoethylphosphonic and 1-aminoethylphosphonous acids were able to be hydrolyzed with high concentrations of penicillin acylase in a reasonable time period. This finding was used to prepare both L- and D-enantiomers of these phosphorus analogues of alanine by stepwise enzymatic hydrolysis of their racemic N-phenylacetyl derivatives using the same enzyme - penicillin acylase - by simply changing the enzyme/substrate ratio.