Abstract
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 KCl caused only a slight reversible inhibition, in contrast to the complete inactivation exerted on the mammalian SAHase.
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