Enzyme Activity Measurement of NAD+ Kinase Using Spectrophotometric Assays

Creative Enzymes has rapidly evolved to one of the most professional enzyme service companies in the world. We have focused on transferases activity testing for several years. Relying on the advanced equipment and the extensive experiences, our experts are able to provide the most suitable activity services for NAD⁺ kinase.

NAD⁺ kinase (NADK, EC 2.7.1.23) catalyzes the phosphorylation from nicotinamide adenine dinucleotide (NAD⁺) to NADP⁺, using ATP as the phosphate group donor. NADKs have been identified in bacteria, plants, vertebrates, and humans. NADKs form a multimeric state in solution and divalent metals, usually magnesium, are essential for carrying out their activities.

The catalytic reaction is universal in organisms because it is the only reaction known to yield NADP⁺. The product NADP⁺ is an essential coenzyme in vivo. The most prominent function of NADP⁺ is the maintenance of a pool of reducing equivalents for metabolic systems that protect the cell from damage. Furthermore, NADPH, the reduced form of NADP⁺, is essential to the regeneration of all known oxidative defense systems, such as glutathione, thioredoxin, and peroxiredoxins. In addition, NADPH provides the reducing power in biosynthetic processes such as fatty acid biosynthesis and nucleotide synthesis. Due to the participation in the critical progresses of growth and the relation to hyper proliferation, NADK has become an attractive target for cancer therapy. Studies have shown that thionicotinamide and other nicotinamide analogs are potential inhibitors of NADK, and the treatment of colon cancer cells with thionicotinamide seems to be effective. To find more potential drugs for the clinical treatment, a large amount research has been carried out to screen high specificity inhibitors. In this process, reliable activity determination is the key step to characterize the enzyme and identify inhibitors. Creative Enzymes has demonstrated the ability to perform reliable and suitable activity assays for NAD⁺ kinase that meet any research purpose.

Figure: The crystal structure of a NAD+ kinase from Archaeoglobus fulgidus in complex with NAD⁺.
Reference: Liu, J. et al. J.Mol.Biol. 2005 354: 289-303.

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