NADP binding

Definition

Target type: molecularfunction

Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. [GOC:ai]

NADP+ binding is a fundamental molecular function that involves the specific and reversible interaction of proteins with nicotinamide adenine dinucleotide phosphate (NADP+). This interaction plays a crucial role in various metabolic pathways, particularly those involving redox reactions. NADP+ serves as a cofactor for a diverse array of enzymes, primarily dehydrogenases, that catalyze oxidation-reduction reactions. The binding of NADP+ to these enzymes is essential for their catalytic activity and involves specific interactions between the cofactor and the enzyme's active site. These interactions often involve hydrogen bonding, electrostatic interactions, and hydrophobic interactions. Upon binding, NADP+ undergoes a conformational change, which allows it to accept or donate electrons during the enzymatic reaction. The transfer of electrons is facilitated by the nicotinamide ring of NADP+, which can exist in two redox states: oxidized (NADP+) and reduced (NADPH). The reduced form, NADPH, is a potent reductant and serves as a source of electrons for various biosynthetic and anabolic processes, such as fatty acid synthesis and steroid biosynthesis. In contrast, the oxidized form, NADP+, is involved in catabolic pathways, such as the pentose phosphate pathway, which generates NADPH and reducing equivalents for biosynthesis. The specificity of NADP+ binding is crucial for maintaining the proper direction and efficiency of metabolic pathways. Mutations or alterations in the binding site can disrupt enzyme activity and lead to metabolic dysregulation. NADP+ binding is a highly conserved molecular function across different organisms, highlighting its critical role in cellular metabolism.'
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Proteins (22)

Compounds (263)