N- 2-hexyl glycine methyl ester | 137132-04-8

• 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- 2-hexyl glycine methyl ester
• 英文别名: N-[methoxy (1-N-benzyloxycarbonylaminoethyl)phosphinyl] 2-hexyl glycine methyl ester
• CAS: 137132-04-8；137173-67-2；137173-68-3；137173-72-9
• 化学式: C₂₀H₃₃N₂O₆P
• 分子量: 428.466
• InChiKey: QZIPWEQTBFIJKS-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.2
• 重原子数：
  29.0
• 可旋转键数：
  13.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.6
• 拓扑面积：
  102.96
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  N- 2-hexyl glycine methyl ester 在 sodium hydroxide 作用下， 反应 24.0h， 生成 N- 2-hexylglycine disodium salt
  参考文献：
  名称：

  Time-dependent inhibition of Streptococcus faecalisd-alanine: d-alanine ligase by α-aminophosphonamidic acids

  摘要：

  Some alpha-aminophosphonamidates which may mimic the transition state of D-alanine: D-alanine ligase catalytic reaction have been synthesized. The inhibition of the ligase by these compounds was investigated with Streptococcus faecalis enzyme using [C-14]-D-Ala assay. Apparent K(i) values analyzed by Dixon plots are in the same range as the apparent K(m). These compounds exhibit a time-dependent inhibition in the presence of ATP, suggesting that they undergo phosphorylation prior to inactivating the enzyme. The (enzyme-inhibitor-ATP) complex apparently dissociates very slowly, showing a process of slow binding inhibition. These results are consistent with the mechanistic model recently postulated for the inhibition of the ligase of Salmonella typhimurium by phosphinic acids.

  DOI：

  10.1016/0223-5234(91)90057-t
• 作为产物：
  描述：

  N-benzyloxycarbonyl-1-aminoethanephosphonic acid methyl monoester 在 氯化亚砜 、 三乙胺 作用下， 以 氯仿 为溶剂， 反应 5.0h， 生成 N- 2-hexyl glycine methyl ester
  参考文献：
  名称：

  Time-dependent inhibition of Streptococcus faecalisd-alanine: d-alanine ligase by α-aminophosphonamidic acids

  摘要：

  Some alpha-aminophosphonamidates which may mimic the transition state of D-alanine: D-alanine ligase catalytic reaction have been synthesized. The inhibition of the ligase by these compounds was investigated with Streptococcus faecalis enzyme using [C-14]-D-Ala assay. Apparent K(i) values analyzed by Dixon plots are in the same range as the apparent K(m). These compounds exhibit a time-dependent inhibition in the presence of ATP, suggesting that they undergo phosphorylation prior to inactivating the enzyme. The (enzyme-inhibitor-ATP) complex apparently dissociates very slowly, showing a process of slow binding inhibition. These results are consistent with the mechanistic model recently postulated for the inhibition of the ligase of Salmonella typhimurium by phosphinic acids.

  DOI：

  10.1016/0223-5234(91)90057-t