N²-phenylacetyl-asparagine | 2752-49-0

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: N²-phenylacetyl-asparagine
• 英文别名: N²-Phenylacetyl-asparagin；Phenacetyl-asparagin；4-Amino-4-oxo-2-[(2-phenylacetyl)amino]butanoic acid
• CAS: 2752-49-0
• 化学式: C₁₂H₁₄N₂O₄
• mdl: MFCD00136895
• 分子量: 250.254
• InChiKey: OXZNUVREVMKPPC-UHFFFAOYSA-N

物化性质

• 熔点：
  189-190 °C(Solv: water (7732-18-5))
• 沸点：
  634.8±55.0 °C(Predicted)
• 密度：
  1.317±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.4
• 重原子数：
  18
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  110
• 氢给体数：
  3
• 氢受体数：
  4

安全信息

• 海关编码：
  2924299090

反应信息

• 作为反应物：
  描述：

  N²-phenylacetyl-asparagine 在 盐酸 、 甲醇 、 penicillin G acylase from Escherichia coli 、 水 作用下， 以 aq. phosphate buffer 为溶剂， 反应 30.5h， 生成 (S)-1-(N-phenylacetylamino)-2-carbamoylethylphosphonic acid
  参考文献：
  名称：

  Penicillin G acylase-mediated kinetic resolution of racemic 1-( N -acylamino)alkylphosphonic and 1-( N -acylamino)alkylphosphinic acids and their esters

  摘要：

  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.

  DOI：

  10.1016/j.molcatb.2016.05.011
• 作为产物：
  描述：

  DL-天冬酰胺一水物 、 苯乙酰氯 在 alkali 作用下， 生成 N²-phenylacetyl-asparagine
  参考文献：
  名称：

  Shiple; Sherwin, Journal of Biological Chemistry, 1922, vol. 53, p. 472

  摘要：

  DOI：

文献信息

• Preparation of d-amino acids by enzymatic kinetic resolution using a mutant of penicillin-G acylase from E. coli
  作者：Chiara Carboni、Hans G.T. Kierkels、Lucia Gardossi、Kamil Tamiola、Dick B. Janssen、Peter J.L.M. Quaedflieg

  DOI：10.1016/j.tetasy.2005.12.023

  日期：2006.1

  We have demonstrated for the first time that D-glutamine (D-Gln) and D-glutamic acid (D-Glu) can be efficiently obtained in high ee (97% and 90%, respectively) by enzymatic kinetic resolution of D,L-Gln and D,L-Glu. This was achieved by enantioselective conversion of the L-enantiomers to their N-phenylacetyl derivatives in aqueous solution, using a mutant of penicillin-G acylase (PGA) from E coli and phenylacetic acid methylester as the acyl donor. Kinetic modeling studies suggest that the high ee values obtained are both due to a strong enantiopreference for the L-amino acid in the deacylation step of the covalent enzyme intermediate, as well as to completeness of conversion that is transiently obtained as a result of the distinct preference of the mutant PGA for phenylacetic acid methylester over the N-phenylacetyl-L-amino acid product. For the other amino acids tested (Asn, Asp, and Ser), the highest ee values that were obtained for the remaining D-enantiomer are moderate (50-80%)because of lower enantioselectivity in the enzyme deacylation step and due to less complete conversion of the L-amino acid caused by competition for the active site between the acyl donor and the N-phenylacetyl-L-amino acid that is produced. The results demonstrate that the mutated PGA has great potential for the production of optically active D-amino acids by kinetic resolution. (c) 2006 Published by Elsevier Ltd.
• Thierfelder; Sherwin, Chemische Berichte, 1914, vol. 47, p. 2632
  作者：Thierfelder、Sherwin

  DOI：——

  日期：——
• ALPHA-AMIDES OF(L)-AMINO ACIDS AS FRAGRANCE PRECURSORS
  申请人：The Gillette Company

  公开号：EP1052968B1

  公开（公告）日：2007-12-05
• 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.
• Shiple; Sherwin, Journal of Biological Chemistry, 1922, vol. 53, p. 472
  作者：Shiple、Sherwin

  DOI：——

  日期：——