Abstract
S-Adenosyl-l-homocysteine (AdoHcy) hydrolase is crucial for the maintenance of biomethylation. The usual mechanistic sequence involves oxidation of AdoHcy at C3‘ followed by elimination of l-homocysteine, Michael addition of water, and reduction to give adenosine. A 6‘-fluorohomovinyladenosine analogue (EDDFHA) undergoes hydration of the 5‘,6‘ double bond (hydrolytic activity) at a more rapid rate than oxidation at C3‘. Three 4‘,5‘-didehydro-5‘-deoxy-5‘-fluoro nucleoside analogues were prepared from 3‘-deoxy- and 3‘-(chloro and fluoro)-3‘-deoxyadenosine via generation of the vinyl fluorides by thermolysis of 5‘-fluoro-5‘-thioether sulfoxides. The 3‘-deoxy analogues of 6‘-halohomovinyladenosines were prepared by Wittig extension with a 3‘-deoxy-5‘-carboxaldehyde and halodestannylation of vinyl stannanes. The 3‘-hydroxyl group appears to be essential for binding to AdoHcy hydrolase. No hydrolytic activity at C5‘ or C6‘ was observed with the nonoxidizable 3‘-deoxy or 3‘-(chloro or fluoro) analogues in contra...
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