Abstract
Four potential S-adenosyl- l-homocysteine hydrolase inhibitors were prepared and tested against purified recombinant rat liver enzyme. Preliminary studies indicate that three of these compounds, 1, 2, and 4, caused time-dependent inactivation of S-adenosyl- l-homocysteine hydrolase but showed a biphasic nature. Compound 3 was found to be a rapid equilibrium inhibitor of this enzyme.
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