Inhibition studies of S-adenosylhomocysteine hydrolase purified from Acinetobacter calcoaceticus ULA-501.
Adenosine analogs previously reported as reversible inhibitors of mammalian S-adenosylhomocysteine hydrolase (SAHase) have been found to exert similar effects on Acinetobacter calcoaceticus ULA-501 enzyme. In addition, two metal coordination compounds, cis-platinum diammine dichloride (cis-DDP) and its trans isomer (trans-DDP), the former well known for its employment in anticancer chemotherapy, were assayed on both bacterial and mammalian SAHases. In our conditions, trans-DDP appeared to be the strongest inhibitor toward both SAHases. Finally, treatment of the bacterial enzyme with a mixture of ATP-Mg acetate and KC1 caused only a slight reversible inhibition, in contrast to the complete inactivation exerted on the mammalian SAHase.
Impagnatiello
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A
Department of Biomedical Sciences and Technology, University of L'Aquila, Italy.
Franceschini
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N
Oratore
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Bozzi
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A
D015762:2-Chloroadenosine / Q000494:pharmacology; D000150:Acinetobacter / Q000201:enzymology*; D043383:Adenosylhomocysteinase; D002945:Cisplatin / Q000494:pharmacology; D003839:Deoxyadenosines / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006867:Hydrolases / Q000037:antagonists & inhibitors* / Q000302:isolation & purification; D007700:Kinetics
D003839:Deoxyadenosines; D004791:Enzyme Inhibitors; D015762:2-Chloroadenosine; C034697:transplatin; D006867:Hydrolases; D043383:Adenosylhomocysteinase; C058118:2'-deoxyadenosine; D002945:Cisplatin