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Updated: Aug 10, 2026
Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)
Published on: December 20, 2010
Inhibition studies of S-adenosylhomocysteine hydrolase purified from Acinetobacter calcoaceticus ULA-501
A Impagnatiello1, N Franceschini, A Oratore
1Department of Biomedical Sciences and Technology, University of L'Aquila, Italy.
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 KC1 caused only a slight reversible inhibition, in contrast to the complete inactivation exerted on the mammalian SAHase.
