Inhibition of S-adenosylhomocysteine hydrolase by purine nucleoside analogues.
To find out potent inhibitors of S-adenosylhomocysteine hydrolase (SAHase), several deazaadenosine analogues synthesized in this laboratory and some naturally occurring nucleoside analogues were examined with SAHases from yellow lupin seeds and rabbit liver. Neplanocin A, an antibiotic, inhibited both enzymes more potently than aristeromycin which was also an antibiotic and known as one of the most potent inhibitors of SAHase. The 3-deazaadenine derivatives (2'-deoxy, arabinosyl, xylosyl) inactivated lupin SAHase as potent as 3-deazaadenosine. Whereas, inhibitory activities of 1-deazaadenosine, its derivatives, and 7-deazaadenosine (tubercidin) were very weak.
D043383:Adenosylhomocysteinase; D006867:Hydrolases / Q000037:antagonists & inhibitors*; D007700:Kinetics; D011684:Purine Nucleosides / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D014372:Tubercidin / Q000031:analogs & derivatives / Q000494:pharmacology
D011684:Purine Nucleosides; C018258:3-deazaadenosine; D006867:Hydrolases; D043383:Adenosylhomocysteinase; D014372:Tubercidin