Synthesis and biological activity of novel S-adenosyl-L-homocysteine hydrolase inhibitors.
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.
Steere
Jennifer A
JA
Department of Chemistry, University of Waterloo, Waterloo, Ontario, Canada N2L 3G1.
Honek
John F
JF
D043383:Adenosylhomocysteinase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000818:Animals; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000493:pharmacokinetics*; D008099:Liver / Q000378:metabolism; D051381:Rats; D013997:Time Factors
D004791:Enzyme Inhibitors; D043383:Adenosylhomocysteinase