N-phenylacetyl-D-Leu methyl ester

• 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: N-phenylacetyl-D-Leu methyl ester
• 英文别名: methyl (2R)-4-methyl-2-[(2-phenylacetyl)amino]pentanoate
• 化学式: C₁₅H₂₁NO₃
• 分子量: 263.337
• InChiKey: YPPQVRQQTPJCDS-CYBMUJFWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  19
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  55.4
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  D-亮氨酸 在 氯磺酸 、 penicillin-G amidase from E_. coli 作用下， 以 甲苯 为溶剂， 反应 53.0h， 生成 N-phenylacetyl-D-Leu methyl ester
  参考文献：
  名称：

  Quantitative enzymatic protection of d-amino acid methyl esters by exploiting ‘relaxed’ enantioselectivity of penicillin-G amidase in organic solvent

  摘要：

  The lower enantio selectivity displayed by penicillin-G amidase (PGA) from E. coli in organic solvent has been exploited for developing a facile, fast and quantitative method for protection of esters of various D-amino acids via N-acylation. The feasibility of the deprotection of the acylated products was also demonstrated by employing PGA from two different sources in aqueous media. Experimental results are in agreement with previous calculations based on in silico models of the enzyme active site. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetlet.2004.10.153

文献信息

• Quantitative enzymatic protection of d-amino acid methyl esters by exploiting ‘relaxed’ enantioselectivity of penicillin-G amidase in organic solvent
  作者：Chiara Carboni、Peter J.L.M. Quaedflieg、Quirinus B. Broxterman、Paolo Linda、Lucia Gardossi

  DOI：10.1016/j.tetlet.2004.10.153

  日期：2004.12

  The lower enantio selectivity displayed by penicillin-G amidase (PGA) from E. coli in organic solvent has been exploited for developing a facile, fast and quantitative method for protection of esters of various D-amino acids via N-acylation. The feasibility of the deprotection of the acylated products was also demonstrated by employing PGA from two different sources in aqueous media. Experimental results are in agreement with previous calculations based on in silico models of the enzyme active site. (C) 2004 Elsevier Ltd. All rights reserved.