New Pathways to NAD+ Discovered in Nicotinamide Riboside Kinase Structures
Author Information
Author(s): Wolfram Tempel, Wael M. Rabeh, Katrina L. Bogan, Peter Belenky, Marzena Wojcik, Heather F. Seidle, Lyudmila Nedyalkova, Tianle Yang, Anthony A. Sauve, Hee-Won Park, Charles Brenner
Primary Institution: Structural Genomics Consortium and Department of Pharmacology, University of Toronto, Toronto, Canada
Hypothesis
Can the structures of human nicotinamide riboside kinases reveal new pathways for NAD+ biosynthesis?
Conclusion
The study identified new pathways to NAD+ through the phosphorylation of nicotinamide riboside and nicotinic acid riboside by human Nrk enzymes.
Supporting Evidence
- The study demonstrated that human Nrk enzymes can phosphorylate both nicotinamide riboside and nicotinic acid riboside.
- Crystal structures revealed essential active site residues for enzyme activity.
- The research suggests that nicotinic acid riboside is a specific substrate for human Nrk enzymes.
Takeaway
Scientists found that certain enzymes can turn a vitamin called nicotinamide riboside into another important molecule, NAD+, which helps cells stay healthy.
Methodology
The researchers solved the crystal structures of human Nrk1 and Nrk2 enzymes and analyzed their substrate specificity.
Digital Object Identifier (DOI)
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