Mechanism of inactivation of S-adenosyl-L-homocysteine hydrolase by 5'-deoxy-5'-S-allenylthioadenosine and 5'-deoxy-5'-S-propynylthioadenosine.
5'-Deoxy-5'-S-allenylthioadenosine 1 and 5'-deoxy-5'-S-propnylthioadenosine 2, derived from adenosine, were prepared. 1 and 2 caused irreversible inactivation of AdoHcy hydrolase. ESI mass spectra analysis of the inactivated enzyme demonstrated that 1 and 2 were type II "mechanism-based" inhibitors.
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Laboratoire des Réactions Sélectives et Applications-UMR 6519, Université de Reims, BP 1039, 51687 Reims, France.
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Witkowski-Vandenplas
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D000241:Adenosine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000494:pharmacology*; D043383:Adenosylhomocysteinase; D004789:Enzyme Activation / Q000187:drug effects; D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology*; D006801:Humans; D006867:Hydrolases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D007700:Kinetics; D009243:NAD / Q000378:metabolism; D010920:Placenta / Q000201:enzymology
C442680:5'-Deoxy-5'-S-allenylthioadenosine; C442679:5'-deoxy-5'-S-propnylthioadenosine; D004791:Enzyme Inhibitors; D009243:NAD; D006867:Hydrolases; D043383:Adenosylhomocysteinase; D000241:Adenosine