Isolation and characterization of a novel adenosine deaminase inhibitor, IADA-7, from Bacillus sp. J-89.
Lee, G; Lee, SS; Kay, KY; Kim, DW; Choi, S; Jun, HK
Journal of enzyme inhibition and medicinal chemistry, 24(1):59-64, 2009
Journal of enzyme inhibition and medicinal chemistry
Adenosine deaminase (ADA), an enzyme involved in purine metabolism, catalyzes the hydrolytic breakdown of adenosine into inosine and free ammonia. ADA regulation has been targeted as a potential therapeutic agent for viral infections and lymphoproliferative disorders. In this study, we isolated a novel ADA inhibitor from a culture of Bacillus sp. J-89, and evaluated its anti-proliferative activity on human cancer cell lines. The ADA inhibitor was deduced as a 2-N-methyl-2,4-diazacycloheptanone by analyses of UV, IR, EI-MASS, (1)H-NMR, (13)C-(1)H NMR, and (13)C-NMR spectroscopy, and was designated IADA-7. IADA-7 was shown to inhibit purified mammalian and Actinomyces ADA. IADA-7 also inhibited the proliferation of both Jurkat T cells (IC(50) = 15 microg/mL) and J 82 (human transitional-cell carcinoma, bladder) cells (IC(50) = 25 microg/mL). In Jurkat T cells, apoptosis with 15 microg/mL IADA-7 for 24 and 48 hours was 9 and 13%, respectively. These results suggest that IADA-7 can inhibit ADA activity in multiple species and that it may represent a good candidate as an anti-cancer therapeutic agent due to its demonstrated anti-proliferative activity on cancer cells.
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