Interaction Between Renalase and Molecules to Regulate Cellular Energy: Preclinical Findings

Synopsis

Renalase is an enzyme that helps convert unusual forms of NADH and NADPH—called 2- and 6-isomers—back into their normal active forms, NAD+ and NADP+. These unusual forms can block other important enzymes in metabolism, so renalase helps keep cellular processes running smoothly. The study shows how renalase interacts with different molecules: some, like nicotinamide nucleosides and mononucleotides, can act as weak substrates, while normal NADH and NADPH compete more effectively for the enzyme’s active site. For human renalase, the enzyme binds 6-dihydronicotinamide riboside much better when ADP is present, but adding similar helper molecules generally doesn’t improve the reaction. Overall, the findings help explain how renalase selectively targets harmful NADH/NADPH isomers to prevent metabolic disruption.

Journal

Archives of Biochemistry and Biophysics