bis(3-oxapentadecyl)-L-glutamate hydrochloride | 133622-39-6

• 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: bis(3-oxapentadecyl)-L-glutamate hydrochloride
• 英文别名: bis(2-dodecoxyethyl) (2S)-2-aminopentanedioate;hydrochloride
• CAS: 133622-39-6
• 化学式: C₃₃H₆₅NO₆*ClH
• 分子量: 608.343
• InChiKey: CZAZSSFIZKYBKT-YNMZEGNTSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8.48
• 重原子数：
  41
• 可旋转键数：
  34
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.94
• 拓扑面积：
  97.1
• 氢给体数：
  2
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  bis(3-oxapentadecyl)-L-glutamate hydrochloride 在 氰基磷酸二乙酯 、 三乙胺 、 三氯氧磷 作用下， 以 四氢呋喃 为溶剂， 反应 75.5h， 生成 O,O-bis(3-oxapentadecyl)-N-(11-phosphoroxyundecanoyl)-L-glutamate
  参考文献：
  名称：

  Functional conversion of myoglobin bound to synthetic bilayer membranes: from dioxygen storage protein to redox enzyme

  摘要：

  Myoglobin (Mb), a water-soluble hemoprotein, is effectively organized together with NADH and FMN coenzymes on the surface of aqueous synthetic bilayer membranes. The redox activity and the binding mode of membrane-bound Mb molecules were studied by UV-visible and ESR spectroscopies and the ultrafiltration binding assay. Mb molecules bound onto a mixed bilayer of ammonium (1) and phosphate (2) amphiphiles can efficiently accept an electron from NADH via FMN and subsequently release its electron catalytically to dioxygen and 1,2-naphthoquinone-4-sulfonate. Thus, Mb is converted from an oxygen storage protein to a redox enzyme. ESR examination of a cast film of the aqueous mixture indicates that Mb is bound to the mixed bilayer in a precision comparable to conventional membrane-bound enzymes. Implications of the present methodology were discussed in terms of functional conversion of enzymes and design of novel multienzyme systems.

  DOI：

  10.1021/ja00025a031

文献信息

• Functional conversion of myoglobin bound to synthetic bilayer membranes: from dioxygen storage protein to redox enzyme
  作者：Itaru Hamachi、Shunsaku Noda、Toyoki Kunitake

  DOI：10.1021/ja00025a031

  日期：1991.12

  Myoglobin (Mb), a water-soluble hemoprotein, is effectively organized together with NADH and FMN coenzymes on the surface of aqueous synthetic bilayer membranes. The redox activity and the binding mode of membrane-bound Mb molecules were studied by UV-visible and ESR spectroscopies and the ultrafiltration binding assay. Mb molecules bound onto a mixed bilayer of ammonium (1) and phosphate (2) amphiphiles can efficiently accept an electron from NADH via FMN and subsequently release its electron catalytically to dioxygen and 1,2-naphthoquinone-4-sulfonate. Thus, Mb is converted from an oxygen storage protein to a redox enzyme. ESR examination of a cast film of the aqueous mixture indicates that Mb is bound to the mixed bilayer in a precision comparable to conventional membrane-bound enzymes. Implications of the present methodology were discussed in terms of functional conversion of enzymes and design of novel multienzyme systems.