Kitade Y, Kozaki A, Miwa T, Nakanishi M, Yatome C
Laboratory of Molecular Biochemistry, Department of Biomolecular Science, Faculty of Engineering, Gifu University, Yanagido 1-1, Gifu 501-1193, Japan.
Nucleic Acids Symp Ser. 2000(44):111-2. doi: 10.1093/nass/44.1.111.
The cellular enzyme S-adenosyl-L-homocysteine (SAH) hydrolase has emerged as a target enzyme for the molecular design of anti-viral agents. Recently, SAH hydrolase has been considered as an attractive target in parasite chemotherapy for malaria. We report synthesis of several carbocyclic purine nucleosides and their inhibitory activities against human and malaria recombinant SAH hydrolases.
细胞酶S-腺苷-L-高半胱氨酸（SAH）水解酶已成为抗病毒药物分子设计的靶标酶。最近，SAH水解酶被认为是疟疾寄生虫化疗中一个有吸引力的靶点。我们报道了几种碳环嘌呤核苷的合成及其对人和疟疾重组SAH水解酶的抑制活性。
