A conceptual model of the polyamine binding site of N1-acetylpolyamine oxidase developed from a study of polyamine derivatives |
| |
Authors: | Takao Koichi Shibata Satoko Ozawa Tomohiro Wada Makiko Sugitia Yoshiaki Samejima Keijiro Shirahata Akira |
| |
Institution: | (1) Faculty of Pharmaceutical Sciences, Josai University, 1-1 Keyakidai, Sakado Saitama, 350-0295, Japan |
| |
Abstract: | We used various polyamine derivatives to study the substrate binding site of N
1-acetylpolyamine oxidase (PAO) that was partially purified from rat liver. The substrate activities of acetylpolyamines indicated
the presence of two anionic centers corresponding to the 1,3-diaminopropane (1,3-DAP) structure and a hydrophobic region in
addition to the cleavage site of the acetamidopropyl group. Based on the results of the inhibitory activities of 1,3-DAP derivatives,
we developed a conceptual model of the polyamine binding site of PAO. We used this model to identify a potent competitive
inhibitor, N
1,N
7-dihexyl-1,7-diamino-4-azaheptane, and to develop an affinity column, 1,16-diamino4,13-diazahexadecane–linked Sepharose, which
was useful for the purification of PAO. |
| |
Keywords: | |
本文献已被 PubMed SpringerLink 等数据库收录! |
|