NAD+ kinase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: ATP + NAD+ = ADP + 2 H+ + NADP+. [EC:2.7.1.23, RHEA:18629]

NAD+ kinase activity is a crucial enzymatic function involved in the biosynthesis of NADP+ from NAD+. This process occurs in both prokaryotic and eukaryotic cells, playing a significant role in various cellular processes. NADP+ acts as a primary electron acceptor in numerous metabolic pathways, including the pentose phosphate pathway, fatty acid biosynthesis, and the reduction of oxidized glutathione. The enzyme responsible for this activity, NAD+ kinase, catalyzes the transfer of a phosphate group from ATP to the 2'-hydroxyl group of the adenosine moiety in NAD+, resulting in the formation of NADP+. This phosphorylation reaction is highly specific and requires the presence of both NAD+ and ATP as substrates. NAD+ kinases are typically found in the cytoplasm of cells, although they may also localize to other cellular compartments depending on the organism and the specific isoform. The activity of NAD+ kinase can be regulated by a variety of factors, including the intracellular concentrations of NAD+, ATP, and NADP+. Furthermore, the enzyme's activity can be influenced by the presence of specific inhibitors and activators. The precise mechanism of NAD+ kinase activity varies depending on the specific enzyme, but it generally involves the formation of a transient enzyme-substrate complex that facilitates the transfer of the phosphate group. In summary, NAD+ kinase activity is an essential enzymatic process that plays a key role in the biosynthesis of NADP+, a critical cofactor in numerous metabolic pathways.'
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Proteins (1)

Compounds (3)