Riboflavin:NAD(P)+ oxidoreductase

Riboflavin:NAD(P)+ oxidoreductase refers to a class of enzymes that catalyze redox reactions using riboflavin (vitamin B2) as a substrate and NAD(P)+ (nicotinamide adenine dinucleotide (phosphate)) as a cofactor or electron acceptor. These enzymes belong to the broader oxidoreductase enzyme family, which facilitates the transfer of electrons from one molecule (the reductant, or electron donor) to another (the oxidant, or electron acceptor).

Specifically, riboflavin:NAD(P)+ oxidoreductases catalyze the oxidation of riboflavin or a reduced form of riboflavin, and the concomitant reduction of NAD+, NADP+, or a related nicotinamide nucleotide. The general reaction involves the transfer of electrons from the riboflavin substrate to NAD(P)+, resulting in oxidized riboflavin and reduced NAD(P)H.

These enzymes play crucial roles in various metabolic pathways, often involved in the regeneration of reducing equivalents or in the biosynthesis of essential cofactors. The exact function and substrate specificity can vary significantly depending on the specific enzyme and organism. They are found in a wide range of organisms, including bacteria, fungi, plants, and animals.

The systematic name for enzymes belonging to this class generally follows the form "riboflavin:NAD(P)+ oxidoreductase," followed by a more descriptive name that reflects the specific reaction catalyzed. Further characterization of these enzymes usually involves determining the specific riboflavin derivative substrate, the preferred nicotinamide nucleotide cofactor (NAD+ or NADP+), and the overall metabolic context in which the enzyme functions.