Synthesis of carbocyclic nucleosides and their SAH hydrolase inhibitory activities.
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.
Kitade
Y
Y
Laboratory of Molecular Biochemistry, Department of Biomolecular Science, Faculty of Engineering, Gifu University, Yanagido 1-1, Gifu 501-1193, Japan.
Kozaki
A
A
Miwa
T
T
Nakanishi
M
M
Yatome
C
C
D043383:Adenosylhomocysteinase; D000818:Animals; D000962:Antimalarials / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D006801:Humans; D006867:Hydrolases / Q000037:antagonists & inhibitors*; D066298:In Vitro Techniques; D015394:Molecular Structure; D010963:Plasmodium falciparum / Q000201:enzymology; D011684:Purine Nucleosides / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D011994:Recombinant Proteins / Q000037:antagonists & inhibitors
D000962:Antimalarials; D004791:Enzyme Inhibitors; D011684:Purine Nucleosides; D011994:Recombinant Proteins; D006867:Hydrolases; D043383:Adenosylhomocysteinase